Download CURRICULUM VITAE - NMR Research Centre

CURRICULUM VITAE
Name
: S. RAGHOTHAMA
Address
: NMR Research Centre, Indian Institute of Science,
Bangalore - 560 012, India.
Phone: +91-80-2293 3301 (Off.)
+91-80-2363 3080 (Res.)
Fax:
+91-80-2360 1550
mobile: 9880038337
email : [email protected]
Gender
: Male
Marital Status
: Married
Nationality
: Indian
Academic Career
: MS - Purdue University, USA (1990).
(Thesis: Probing enantiodifferentiation in chiral stationary
phases using NMR spectroscopy and molecular modeling,
(Guide: Prof. K.B. Lipkowitz).
: Ph.D. – IISc, ,Bangalore. India (1998).
(Thesis: Structural motifs in designed synthetic peptides:
NMR characterization)
(Guide : Prof. P. Balaram and Prof. C.L.Khetrapal.).
: Post doctoral Research fellow (1998-2000)
at University of Sheffield, UK,
Protein structure determination using 2D and 3D NMR.
(with Prof. M.P. Williamson).
Positions Held
: Chief Research Scientist
(2014 Principal Research Scientist (2007 - 2014)
Senior Scientific Officer
(2001 - 2007).
at NMR Research Centre, Indian Institute of Science,
Bangalore, India.
Associated with running and maintenance of National
NMR facility since inception from 1977. Currently
houses 7 spectrometers (300 – 800MHz ).
Research Areas
: Bio-structures, NMR methods, metabolomics.
(Highlights attached)
Teaching
: CD301 (Jan.semester every year): ‘Two-dimensional
NMR Spectroscopy.’ under Integrated Ph.D programme
in Chemical Sciences Division of Indian Institute of
Science.
One semester course on ‘NMR Spectroscopy: Practice
and Applications to Biological Systems’. at Centre of
Continuing education (Proficience), Indian Institute of
Science. (Since 2004).
Current Projects
funded by Govt.
: (i) Peptide conformations: Solid state NMR study at
Natural abundance.
(by CSIR,Government of India)
(ii) Structural Investigations of Amyloid Peptide
Fragments Implicated in Alzheimers Disease.
(by DST, India)
Awards /
Recognition
Membership of
Professional Bodies
General Proficiency
: Bruker Young Scientist Award for the year 1989.
Elected as Executive committee member of National
Magnetic Resonance Society. (2007 - 2013) and
nominated as Treasurer.
: Life member - National Magnetic Resonance Society,
Life member - National Academy of Sciences - India.
Life member - Indian Peptide Society, India.
Life member - American Peptide Society- USA.
: Cryogenics: Associated with Central Cyrogenics Facility,
Indian Institute of Science, Bangalore – 560 012, India.
Computers: Molecular Modeling, NMR structure
calculation using commercial softwares.
List of Publications
: 90 publications in international journal (see list enclosed)
Research Highlights
S. Raghothama.
NMR Research Centre, Indian Institute of Science, Bangalore -560012,
India.
NMR analysis of natural and synthetically designed peptides:
NMR spectroscopy is a powerful technique for the study of conformational and structural
aspects of biological molecules. In the use of this methodology various approaches are
possible. Of these, one of the important areas is the study of natural and synthetically
designed peptides which have important roles in controlling biological processes.
Currently scientific investigations are focused on the application of NMR spectroscopy to
conformational and structural aspects of such biomolecules.
State of the art NMR
methodologies have been applied for such studies and detailed structural analysis have
been carried out.
The use of computer based molecular modeling and structure
calculation have also been made. Listed below are some of these studies carried out, part
of which also form collaborative efforts:
(i)
Amyloid peptide fragment analysis.
(ii)
Studies oriented towards drug design based on natural and synthetic peptides.
(iii)
Applications of recent methodological developments in solid state NMR to
peptide structures at natural abundance.
(iv)
Understanding protein folding from synthetic design of specific motifs.
(v)
3D-structure elucidation of proteins and peptides.
(vi)
Metabolomics studies on stem cell growth media.
Following are the highlights of some of these projects:
(i) Amyloid peptide fragment metal
interaction:
(b) Obestatin fragments and its mutant
analysis:
Charged residues in Amyloid A
fragments, A16 and A12 were shown
to be involved in Aluminium binding
rather than the usual histidine residues.
NMR structures with and without
Aluminium was calculated and binding
site identified using modeling. Such
studies are useful in inhibiting amyloid
formation.
Three overlapping 13 residue fragments
along with its mutants of obese control
drug obestatin were characterized by
NMR and found that the N-terminal
fragment and its mutant which has
resistance to proterolytic degradation
almost matched the parent peptide
activity.
(ii) (a) Conus peptides : Contryphans
and its analogs study (Lo-959).
(iii) (a) Natural abundance Solid state
NMR of designed -turn tripeptide
containing Proline residues - cis/trans
distinction.
Contryphans, cyclic Cysteine containing
peptides, extracted from conus toxins are
rich source of molecules towards drug
development projects. Aromatic-proline
interactions influence on structures is
analyzed by detailed NMR experiments.
Two independent cis / trans NMR
structures were calculated. This is a
good example of single molecule
binding to multiple receptors.
Solution and solid state peptide
structures often differs. Solution NMR
resulted in cis and trans forms coexisting in a designed tripeptide (PivPro-Pro-Phe-OMe). Crystal structure of
the same also had two forms but both
were cis. Hence 13C-CPMAS solid state
NMR was carried out which matched
that of crystal structures. The study
shows the power of solid state NMR
which can be used at natural abundance
to derive certain structural features.
(b) SSNMR peptide structures: Use of
single quantum / double quantum
(SQ/DQ) methodology:
a tripeptide
example.
C -1H SQDQ (single quantum double
quantum) correlation experiment again
at natural abundance is well utilized to
spread out the limited 1H chemical shifts
and at the same time identify long range
through space interactions. Use pseudoproline (Pro) to push equilibrium to cis
-turn design is studied. In the
absence of crystal structure, this study
showed presence of both cis and trans
form in the sequence (Piv- Pro-ProLeu-NHMe) in contrast to solution
single form. A details analysis was
carried out along with other connected
peptides with complete assignment
obtained
from
different
edited
experiments of SSNMR.
analyzed. The maintenance of the
specific aromatic ring orientation in
organic solvents provides evidence for
significant stabilizing interaction.
(b) Hybrid peptides: insertion of higher
homologs of amino acids (-
13
Hybrid polypeptide backbones are
potential candidates in protein mimetics.
They provide proteolytically stable
sequences, very useful in drug design
and delivery. Studies show stable
secondary structures with -amino
acids.
(c) Conformation Switch in designed
peptides:
(iv)
(a) Aromatic interactions in
stabilizing -hairpin structures:
In this interesting study a simple
configuration change in central residue
-DVal to LVal allow to analyze
independently simultaneous existence
-hairpin
structures. Such studies are very useful
in understanding amyloid formation
leading
to
serious
diseases.
Diagnostic ring current shift of aromatic
protons in case of Phe-Phe interaction is
LIST OF PUBLICATIONS
(S. Raghothama, NMR Research Centre, IISc. Bangalore)
1. Determination of chemical shift anisotropy of molecules in a mixture of two liquid
crystals of opposite diamagnetic anisotropies.
S. Raghothama
J. Magn. Reson. 57, 294, (1984).
2. Solvent effects on the structure of benzo(b) selenophene oriented in liquid crystals.
N. Suryaprakash, S. Raghothama, C.L.Khetrapal, A.C.Kunwar, M. Baiwir and
L.Liabres.
J. Organometallic Chemistry, 277, 359, (1984)
3. Solid state and solution conformation of Boc-L-Met-Aib-L-Phe-OMe -turn
conformation of a sequence related to an active chemotatic peptide analog.
R. Bardi, A.M. Piazzesi, C. Toniolo, P. Antony Raj, S. Raghothama and P.Balaram.
Int. J. Peptide Protein Res. 27, 229, (1986).
4. Conformation of the amino terminal tetrapeptide of emerimicins and antiamoebins in
solution and in the solid state.
R. Bardi, A.M. Piazzesi, C. Toniolo, P. Antony Raj, S. Raghothama and P.Balaram.
Int. J. Biol. Macromol, 8, 201, (1986).
5. Membrane channel forming polypeptide. Molecular conformation and mitochondrial
uncoupling activity of antiamoebin, an -amino-isobutyric acid containing peptide.
Manoj K.Das, S. Raghothama and P. Balaram.
Biochemistry, 25, 7110, (1986).
6. The r-structure, chemical shift anisotropy and the abnormal orientation of
methyldichlorophosphine from NMR spectrum.
C.L. Khetrapal, S. Raghothama and N. Suryaprakash.
J. Magn. Reson., 71, 140, (1987).
7. Cystine peptides, spectroscopic studies on conformation of a cyclic pentapeptide
disulfide.
R. Kishore, S. Raghothama and P. Balaram.
Int. J. Peptide Protein Res. 29, 381, (1987).
8. Cystine peptides. The Intramolecular antiparallel -sheet conformation of a 20membered cyclic peptide disulfide.
R. Kishore, S. Raghothama and P. Balaram.
Biopolymers, 26, 873, (1987).
9. A 1H NMR study of billirubin IX and solubilisation of cholate micelles. An
application of nuclear Overhauser effect.
Kasturi Lahiri Puranam, S. Raghothama and P. Balaram.
Biochem.Biophys. Acta. 922, 67, (1987).
10. Synthetic peptide models for the redox active disulfide loop of glutaredoxin.
Conformational studies.
R. Kishore, S. Raghothama and P. Balaram
Biochemistry, 27, 2462, (1988).
11. Strong coupling and flip angle dependence of coupling patterns in heteronuclear shift
correlation two-dimensional NMR spectra.
V.V. Krishnan, S. Raghothama and Anil Kumar.
J. Magn. Reson., 79, 328, (1988).
12. Oriented molecules.
C.L. Khetrapal, B.S. Arunkumar and S. Raghothama., in “Nuclear Magnetic
Resonance” Ed. G.A.Webb. (Specialist Periodical Reports). The Royal Society of
Chemistry, London., 17, (1988).
13. Cyclic cystine peptides. Antiparallel -sheet conformation for the 20 membered ring
in Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe
|
|
S-------------------------S
Isabella L. Karle, R.Kishore, S. Raghothama and P. Balaram.
J. Am. Chem. Soc., 110, 1958 (1988).
14. Simultaneous observation of positive and negative nuclear Overhauser effects in
oligopeptide due to segmental motion.
K. Uma, H. Balaram, S. Raghothama and P. Balaram.
Biochem. Biophys. Res. Comm. 151, 153, (1988).
15. 13C-NMR studies of discotics.
C.L.Khetrapal. S. Raghothama, N. Suryaprakash and A.C. Kunwar.
Liquid Crystals, 3, 413, 1988.
16. Conformational analysis of cyclolinopeptide A, a cyclic nonapeptide. Nuclear
Overhauser effect and energy minimisation studies.
S. Raghothama, C. Ramakrishnan, D. Balasubramanian and P. Balaram.
Biopolymers, 28, 573, (1989).
17. Nuclear magnetic resonance and thermal studies of drug doped dipalmitoyl
phosphatidyl choline-H2O systems.
K. Usha Deniz, P.S. parvathanathan, Geetha Datta, C.L. Khetrapal,
K.V. Ramanathan, N. Suryaprakash and S. Raghothama.
J. Biosci., 15, 117, (1990).
18. Probing enantiodefferentiation using NMR spectroscopy and molecular modeling.
S. Raghothama and K.B.Lipkowitz.
in ‘magnetic Resonance – Current trends’ ed. C.L. Khetrapal and G.Govil.,
Narosa Publishing House, New Delhi, pp 197-215, (1991).
19. Enantioselective Binding of Tryptophan by -Cyclodextrin.
K.B. Lipkowitz, S. Raghothama and J. Yang.
J. Am. Chem. Soc. 114, 1554, (1992).
20. Lysozyme-DPPC interaction in the model membrane, DPPC-H2O.
P.S. Parvathanathan, Geetha Datta, E.B. Mirza, Lata Sumanan, K. Usha Deniz,
K.V.Ramanathan, S. Raghothama, N. Suryaprakash and C.L. Khetrapal.
J. Surface Sci. Technol., 8, 29, (1992).
21. Structural studies of o-Vanillin derivatives and their metal complexes by 1 and 2D
NMR.
G.A. Naganagowda, S. Raghothama, B.V. Agarwala and C.L. Khetrapal.
Bull. Magn. Reson., 18, 81-84, 1995.
22. A designed -hairpin peptide.
Satish K Awasthi, S. Raghothama and P. Balaram.
Biochem. Biophys. Res. Comm., 216, 375, (1995).
23. Determination of Aib residue conformation in peptides using diagnostic sidechainbackbone Nuclear Overhauser effects.
S. Raghothama, Manjula Chaddha and P. Balaram.
Proc. Natl. Acad. Sci. India., 66 (A) Spl. Issue. 33, (1996).
24. Conformational variability in short acyclic peptides. Stabilisation of multiple -turn
structures in organic solvents.
Satish Kumar Awasthi, S. Raghothama and P. Balaram.
J. Chem. Soc., perkin Trans. 2, 2701-2706 (1996)
25. Ambidextrous Molecules: Cylindrical peptide structures formed by fusing left and
right handed helices.
Arindam Banerjee, SrinivasaRao Raghothama, Isabella L. Karle and
Padmanabhan Balaram.
Biopolymers, 39, 279-285 (1996).
26. NMR analysis of a conformational trasition in an acyclic peptide. A model system
for studying helix unfolding.
S. Raghothama, M. Chaddha and P. Balaram.
J. Phys. Chem., 100, 19666-19671 (1996).
27. Peptide design. Helix-helix motifs in synthetic sequences.
Arindam Banerjee, S. Raghothama and P. Balaram
J. Chem. Soc. Perkin Trans. 2, 2087-2094 (1997).
28. Stereochemical analysis of higher , -dialkylglycine containing peptides.
Characterisation of local helical conformations at Dipropylglycine residue and
observation of a novel hydrated multiple -turn structure in crystals of a glycine rich
peptide.
I.L. Karle, Ramesh Kaul, R. Balaji Rao, S. Raghothama and P. Balaram.
J. Am. Chem. Soc., 119, 12048-12054 (1997).
29. Conformational interconversions in peptide -turns. Discrimination between
enantiomeric conformations by chiral perturbation.
S. Raghothama, Manjula Chaddha, S. Banumathi, Krishna Ravikumar,
D. Velumurugan and P. Balaram.
Biopolymers, 45, 191-202, (1998).
30. -hairpin nucleation by Pro-Gly -turns. Comparison of D-Pro-Gly and L-Pro-Gly
sequences in an apolar octapeptide.
S. Raghothama, S.K. Awasthi and P. Balaram.
J. Che. Soc. Perkin Trans. 2, 137-143 (1998).
31. A designed three stranded -sheet peptide.
C.Das, S. Raghothama and P. Balaram.
J. Am. Chem. Soc. Communication, 120, 5812, (1998).
32. A four stranded -sheet structure in a designed, synthetic polypeptide.
Chittaranjan Das, S. Raghothama, and P. Balaram
Chem. Commun., 967-968, (1999)
33. Solution structure of the CBM10 cellulose binding module from Pseudomonas
xylanase A.
S. Raghothama, Peter J. Simpson, Lorand Szabo, Tibor Nagy, Harry J. Gilbert, and
Michael P. Williamson.
Biochemistry, 39 (5), 978-984, (2000).
34. Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase:
cloning, expression and binding studies.
Maher Abou Hachem, Eva Nordberg Karlsson, Eva Bartonek-Roxa,
Srinivasarao Raghothama, Peter J. Simpson, Harry J. Gilbert, Michael P. Williamson
and Olle Holst.
Biochem. J., 345, 53-60 (2000).
35. Synthetic protein design: Construction of a four stranded -sheet structure and
evaluation of its integrity in methanol-water mixtures.
Chittaranjan Das, V. Nayak, S. Raghothama and P. Balaram
J. Peptide Res. 56, 307-317, (2000).
36. Solvent induced -hairpin to helix conformational transition in a designed peptide.
S.K. Awasthi, S.C. Shankaramma, S. Raghothama and P. Balaram
Biopolymers, 58, 465-476, (2001).
37. Characterisation of a cellulosome dockerin domain from the anaerobic fungus
Piromyces equi
S. Raghothama, Ruth Y. Eberhardt, Peter Simpson, Darran Wigelsworth,
Peter White, Geoffrey P. Hazlewood, Tibor Nagy, Harry J. Gilbert &
Michael P. Williamson
Nature Structure Biology, 8, 775-778, (2001)
38. Clostridium thermocellum Xyn10B carbohydrate –binding module 22-2: The role of
conserved amino acids in ligand binding.
Hefang Xie, Harry J. Gilbert, Simpson J. Charnock, Gideon J. Davies, Michael P
Williamson, Peter J. Simpson, S. Raghothama, Carlos M.G.A. Fontes, Fernando M.
V. Dias, Luis M. A. Ferreira, and David N. Bolam.
Biochemistry, 40, 9167-9176, (2001).
39.  – Hairpins generated from hybrid peptide sequences containing both
 – and  – amino acids.
H.N. Gopi, R.S.Roy. S. Raghothama, I.L. Karle and P. Balaram
Helvetica Chimica Acta, 85, 3313- 3330, (2002).
40. Two Novel Hexadepsipeptide with several modified amino acid residues isolated
from the fungus Isaria.
G. Ravindra, R. S. Ranganyaki, S. Raghothama, M.C. Srinivasan, R.D. Gilardi,
I.L. Karle and P. Balaram.
Chemistry and Biodiversity, 1, 489-504, (2004).
41. hybrid peptides: A polypeptide helix with a central segment containing two
consecutive -amino acid residues.
R.S. Roy, I.L. Karle, S. Raghothama, and P. Balaram.
Proc. Natl. Acad. Sci. (USA), 101, 16476-16482, (2004).
42. NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120
in methanol and water.
Kausik Chakraborty, P. Shivakumar, S. Raghothama & Raghavan Varadarajan
Biochem. J. 390, 573-581, (2005).
43 Tryptophan-containing peptide helices: interactions involving the indole sidechain
R.Mahalakshmi. A. Sengupta, S. Raghothama N. Shamala P. Balaram.
J.Peptide Res. 66, 277-296, 2005.
44 Peptide Hairpins with Strand Segments Containing - and - Amino Acid Residues:
Cross-Strand Aromatic Interactions of Facing Phe Residues.
R.S.Roy , H.N. Gopi, S. Raghothama, R.D.Gilardi,, I.L.Karle,, P. Balaram
Peptide Science (Biopolymers), 80, 787-799, 2005.
45 NMR Analysis of Aromatic Interactions in Designed Peptide - Hairpins.
R. Mahalakshmi, S. Raghothama, P.Balaram.
J. Am. Chem. Soc, 128, 1125-1138, 2006.
46 Design of a Peptide Hairpin Containing a Central Three-Residue Loop
R. Rai, S. Raghothama, and P. Balaram
J. Am. Chem. Soc. 128, 2675-2681, 2006
47 Hybrid peptide Hairpins Containing - and -Amino Acids: Conformational
Analysis of Decapeptides with Unsubstituted --and -Residues at Positions 3and 8.
R.S. Roy, H.N. Gopi, S. Raghothama, I.L. Karle, and P. Balaram.
Chem. Eur. J. 12, 3295-3302, 2006.
48 Diproline Templates as Folding Nuclei in Designed Peptides. Conformational
Analysis of Synthetic Peptide Helices Containing Amino Terminal Pro-Pro Segments
R.Rai, S.Aravinda, K.Kanagarajadurai, S.Raghothama, N. Shamala, and P. Balaram.
J. Am. Chem. Soc. 128, 7916-7928, 2006.
49 Tryptophan rich peptides: Influence of indole rings on backbone conformation R.
Mahalakshmi, A. Sengupta, S.Raghothama, N. Shamala, P. Balaram
Biopolymers (Peptide Science), 88, 36-54, 2007
50 Tuning the -Turn segment in Designed Peptide -Hairpins: Construction of a Stable
Type I’ -Turn Nucleus and Hairpin-Helix Transition Promoting Segments
R. Rai, S. Raghothama, R. Sridharan, P. Balaram.
Biopolymers (Peptide Science), 88, 350-361, 2007,
51 Tyrosine-heme ligation in Heme-peptide complex: design based on conserved motif
of catalase
Jagdish Rai, S. Raghothama, D. Sahal.
Journal of Peptide Science. 13, 406-412, 2007.
52 De novo design of F containing heme binding peptides.
Jagdish Rai, S. Raghothama, D. Sahal
Chemical Biology and Drug Design. 9, 119-123, 2007
53 Identification and characterization of a library of microheterogeneous
cyclohexadepsipeptides from the fungus Isaria
V. Sabareesh , R.S. Ranganayaki, S. Raghothama, M.P. Bopanna, Hema Balaram,
M.C. Srinivasan and P. Balaram.
J. Natural Products , 70, 715-729, 2007.
54. Isolation, Purification and Characterization of an Antifungal Molecule Produced by
Bacillus licheniformis BC98, and its effect on phytopathogen Magnaporthe grisea.
S.R. Tendulkar, Y.K. Saikumari, V. Patel, S. Raghotama, T.K.Munshi, P. Balaram .
B.B. Chattoo,
Journal of Applied Microbiology. 103, 2331-2339, 2007.
55. Hybrid Peptides: Expanding the  Turn in Peptide Hairpins by the Insertion
of  and Residues
Rai. R, Vasudev. P.G, Ananda, K, Raghothama. S, Shamala. N, Karle, I.L, and
Balaram. P.
Chem. Eur. J. 13, 5917-5926, 2007.
56. Designed peptides with homochiral and heterochiral diproline templates as
conformational constraints.
B. Chatterjee, I.Saha, S. Raghothama, S. Aravinda, R Rai, N. Shamala, P.Balaram.
Chem. Eur. J. 14, 6192-6284, 2008.
57. Multiple Conformational States in Crystals and in Solution in αγ Hybrid
Peptides. Fragility of the C12 Helix in Short Sequences.
Sunanda Chatterjee, Prema G. Vasudev, Kuppanna Ananda, Srinivasarao
Raghothama, Narayanaswamy Shamala, and Padmanabhan Balaram
J. Org. Chem. 73, 6595-6606, 2008
58. Solid State and Solution Conformations of a Hybrid  Hexapeptide.
Characterization of a Backbone Expanded Analog of the -Polypeptide 310- Helix.
Sunanada Chatterjee, Prema G. Vasudev, Srinivasarao Raghothama,
Narayanaswamy Shamala, Padmanabhan Balaram.
Biopolymers (Pept.Sci.), 90, 759-771, 2008.
59. Synthesis of 2-deoxy cyclic and linear oligosaccharides by oligomerization
of monomers
Somak Paul, Srinivasarao Raghothama, Narayanaswamy Jayaraman.
Carbohydrate Research, 344, 177–186, 2009.
60. Expanding the Peptide -Turn in  Hybrid Sequences: 12 Atom Hydrogen Bonded
Helical and Hairpin Turns.
S. Chatterjee, P. G. Vasudev, S. Raghothama, C. Ramakrishnan, N. Shamala, and
P. Balaram.
J. Am. Chem. Soc. 131, 5956-5965, 2009.
61. Natural Abundant Solid State NMR Studies in Designed Tripeptides for
Differentiation of Multiple Conformers.
S. Jayanthi, Bhaswati Chatterjee, S. Raghothama
Biopolymers, 91, 851-860, 2009
62. Conformations of Heterochiral and Homochiral Proline- Pseudoproline Segments in
Peptides. Context Dependent cis-trans Peptide Bond Isomerization
Kantharaju, S. Raghothama, U.S. Raghavender, S. Aravinda, N. Shamala, and
P.Balaram.
Biopolymers (Pept.Sci), 92, 405-416, 2009.
63. Ring Expansion of Oxyglycals. Synthesis and Conformational Analysis of
Septanoside-Containing Trisaccharides.
N.Vijaya Ganesh, S.Raghothama, R. Sonti, and N. Jayaraman.
J. Org. Chem. 75, 215-218, 2010.
64. Helical conformations of hexapetpides containing N-terminal diproline segments.
Kantharaju, S. Raghothama, S. Aravinda, N. Shamala, and P. Balaram.
Biopolymers (Pept.Sci.), 94, 360-370, 2010.
65. Solution conformation of a tetradecapeptide stabilized by two di-n-propyl glycine
residues.
Vijayalekshmi Sarojini, R. Balaji Rao, S. Raghothama, and P.Balaram.
Journal of peptide Science, 16, 430-436, 2010.
66. Chemistry in confined spaces: High-energy conformer of a piperidine derivative is
favored within a water-soluble capsuleplex.
Mintu Porel, Nithyanandhan Jayaraj, S. Raghothama, and V. Ramamurthy.
Org. Lett., 12, 4544–4547, 2010.
67. NMR of Peptides.
S. Raghothama,
Journal of the Indian Institute of Science, 90, 145-161, 2010.
68. Effect of ester chemical structure and peptide bond conformation in fragmentation
pathways of differently metal cationized cyclodepsipeptides.
R. Banerjee, S. Sudarslal, R.S. Ranganayaki, and S. Raghothama
Org. Biomol. Chem., 9, 6234-6245, 2011.
69. NMR structure implications of enhanced efficacy of Obestatin fragment analogs.
B. Krishnarjuna, A. D. Ganjiwale, U.V. Manjappara, S. Raghothama.
Int. J. Pept. Res. Ther. 17, 259-270, 2011.
70. Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and
Aib-Aib segments.
A. Rajagopal, S. Aravinda, S. Raghothama, N. Shamala, P. Balaram.
Peptide Science, 96, 744-756, 2011.
71. Aromatic interactions in model peptide -hairpins: Ring current effects on proton
chemical shifts.
A. Rajagopal, S. Aravinda, S. Raghothama, N. Shamala, P. Balaram.
Peptide Science, 98, 185-194, 2012.
72. Three-component self-assembly of a series of triply interlocked Pd12 coordination
prisms and their non-interlocked Pd6 analogues.
A.K. Bar, S. Raghothama, D.Moon, and P.S. Mujkherjee.
Chem. Eur. J. 18, 3199-3209, 2012.
73. Helix and hairpin nucleation in short peptides using centrally positioned
conformationally constrained dipeptide segments.
S. Chandrappa, S. Aravinda, S. Raghothama. R. Sonti, R. Rai, V.V. Harini,
N.Shamala, and P. Balaram.
Org. Biomol. Chem. 10, 2815-2823, 2012.
74. β-Turn Analogues in Model αβ-Hybrid Peptides: Structural Characterization of
Peptides Containing β2,2Ac6c and β3,3Ac6c Residues.
K. Basuroy, A. Rajagopal, S. Raghothama, N. Shamala , P. Balaram.
Chem. Asian J, 7, 1671-1678, 2012.
75. Theoretical and in vitro studies of a C-terminal peptide from PGKC of Leishmania
mexicana Mexicana.
S. Kaushik, B. Krishnarjuna, S. Raghothama, S. Aggarwal, V. Raghunathan, A.
Ganjiwale.
Mol Biochem Parasitol, 185, 27. 2012.
76. NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14
residue three stranded -sheet peptide.
R. Sonti, R. Rai, S. Raghothama, P. Balaram
J. Phys. Chem. B 116, 14207-14215, 2012
77. Does Aluminium bind to Histidine? An NMR investigation in Aβ12 and Aβ16
fragments.
Priya Narayan, B. Krishnarjuna2, V. Vinaya, D.Jagadeesh Kumar, K.V.
Ramanathan, K.R.K Eswaran, H.G. Nagendra, S. Raghothama.
Chem. Bio. Drug. Des . 82, 48-59, 2013,
78. A Designed Three-Stranded -Sheet in an Hybrid Peptide.
Rajesh Sonti, Hosahudya N. Gopi, Umashankara Muddegowda,
Srinivasarao Ragothama, and Padmanabhan Balaram.
Chem. Eur. J., 19, 5955-5965, 2013.
79. Stabilizing effect of electrostatic vs. aromatic interactions in diproline nucleated
peptide-hairpins.
Kamlesh Madhusudan Makwana,a Srinivasarao Raghothama* and
Radhakrishnan Mahalakshmi*
Phys. Chem. Chem. Phys., 15, 15321-15324, 2013.
80. Unconstrained Homooligomeric γ-Peptides Show High Propensity for C14 Helix
Formation
Krishnayan Basuroy, Bhimareddy Dinesh, M. B. Madhusudana Reddy,
Siddapa Chandrappa,‡ Srinivasarao Raghothama,§ Narayanaswamy Shamala,
and Padmanabhan Balaram.
Org. Lett. 15, 4866-4869, 2013.
81. Conformational Diversity in Contryphans from Conus Venom: cis–trans
Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of
a 7-Residue Peptide Disulfide Loop
Rajesh. S, K. H.Gowd, K. N. Shashanka Rao, S. Ragothama, A.Rodriguez,
J.J. Perez, and P.Balaram.
Chem. Eur. J. 19, 15175-15189, 2013.
82. C12-Helix Development in (αγ)n Sequences – Spectroscopic Characterization of
Boc–[Aib–γ4(R)Val]–OMe Oligomers
B. Dinesh, V.Vinaya, S. Raghothama, and P. Balaram.
Eur. J. Org. Chem., 3590–3596, 2013.
83. C12 Helices in Long Hybrid (αγ)n Peptides Composed Entirely of Unconstrained
Residues with Proteinogenic Side Chains
R. Sonti B. Dinesh, K. Basuroy, S. Raghothama, N. Shamala, and P. Balaram.
Org. Lett. 16, 1656-1659, 2014.
84. Evaluation of hexane and ethyl acetate extracts of the sponge Jaspis diastra collected
from Mauritius Waters on HeLa cells.
G. Beedessee, A.Ramanjooloo, I. Tiscornia, S.Rao, D. Arya, K.H.Gowd, S.
Raghotham, P.Balara, M. B-Fogolin, D. E.P Marie.
Journal of Pharmacy and Pharmacology. (in press), 2014.
85. Conformational Analysis of a 20-Membered Cyclic Peptide Disulfide from Conus
Virgo with a WPW Segment: Evidence for an Aromatic–Proline Sandwich.
R. Sonti, K. N. Shashanka Rao, S. Chidanand, K. Hanumae Gowd, S. Raghothama,
and P. Balaram.
Chem. Eur. J, 20, 5075-5086, 2014.
86. Directing peptide conformation with centrally positioned pre-organized dipeptide
segments: studies of a 12-residue helix and β-hairpin.
S. Chandrappa, M.B. Madhusudana Reddy, R. Sonti, K. Basuroy. S. Raghothama,
P.Balaram.
Amino Acid. 47, 291-301, 2015.
87. Antimicrobial peptides with potential for biofilm eradication: Synthesis and structure
activity relationship studies of Battacin peptides.
De Zoysa GH, Cameron AJ, Hegde VV, Raghothama S, Sarojini V.
J Med Chem. 58, 625-639, 2015.
88. Effects of hydrogen bonding on amide-proton chemical shiftanisotropy in a prolinecontaining model peptide.
K. Pichumani, G. George, S. Hebbar, B. Chatterjee, S. Raghothama.
Chem. Phys. Letts. 627, 126-129, 2015.
89. Effect of methylene group insertions on the structural rigidity of Aib containing
helices
A. Duley , V.Gowda, A. Ganjiwale , S. Raghothama* and G. Ramanathan*
Peptide Science. 104, 720-732, 2015.
90. Exploring Structural Features of Folded Peptide Architectures in the
Construction of Nanomaterials
R. Misra, R. M. Reja, L.V. Narendra, G. George, S. Raghothama and H. N. Gopi.
Chem. Commun., 52, 9597- 9600, 2016.