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Dr. Kishore Raghuvansh
Design, chemical synthesis and structural characterization of peptides of biological relevance

Contact Address:
0172-6665263  (O) and 6665510 (R)

Write-up of research and development interests/focus, past and present goals:

To design, synthesize and elucidate structural characteristics of short linear hybrid peptides comprised of non-coded α-amino acids and un-substituted -amino acid i.e. beta-Ala moiety. We recently reviewed the potentials of beta-Ala residue to design and construct not only bioactive peptides but also unusual protein secondary structural features. The survey revealed strong preference of the beta-Ala residues to adopt distinct tightly-folded gauche (~ +60+20) and/or fully-extended trans (~ +180+20) orientations in hybrid model peptides. The overall results indicated that unusual combinations of the torsion angles of the beta-Ala moiety tend to facilitate novel intramolecular hydrogen bonded ring motifs in peptides.
We are also investigating the conformational characteristics of Thr containing short linear model peptides. Our preliminary results established the existence of unusual intramolecularly hydrogen bonded secondary structures. The solid-state structural analysis of designed model peptides established the existence of two novel side-chain to main-chain intramolecular hydrogen bonds i.e. Ni+1-HO=Ci and Ci+2-HO=Ci type interactions, stabilizing discrete conformational features.

In addition, we are also pursuing experimental as well as theoretical conformational analysis of various immunostimulating/ immunosuppressive peptides and protein inhibitors in order to develop equipotent or more potent peptide analogs/inhibitors. To gain insight into their bio-active conformation(s), we first explore the accessible conformational space via theoretical methods and then supplement the results with experimental 1H NMR and/or CD spectroscopic data.

Significant recognition: Awards, fellowships, international funding of distinction, technologies transferred/licensed etc.:

  • Visiting scientist  :   Under JSPS- INSA Bilateral Exchange Programme (December 1988 --- June 1989)

  • Visiting scientist  :   JSPS  Invitation Fellowship (Long-term) (June 2001 --- April 2002)

(JSPS: Japan Society for the Promotion of Science and INSA: Indian National Science Academy)

Selected list of Publications and Patents:

1. P. Venugopalan and R. Kishore
Antiparallel self-association of a γ,α-hybrid model peptide: More relevance of weak interactions.
Chem. – An Asian Journal (2015), In Press.

2. J. Dhar, P. Chakrabarti, H. Saini, G. P. S. Raghava and R. Kishore
w-turn: A novel b-turn mimic in globular proteins stabilized by main-chain to side-chain C−H×××O interaction.
PROTEINS: Structure, Function & Bioinformatics (2015), Vol. 83, 203-214.  

3. R. Kaur, M. Ramesh, P. V. Bharatam and R. Kishore                                                                                 Self-association behaviour of a novel non-proteinogenic β-strand-mimic in an organic solvent.
J. Phys. Chem. B (2014), Vol. 118, 9199-9208.

4. P.Venugopalan and R. Kishore
Unusual folding propensity of an unsubstituted β,γ-hybrid model peptide: Importance of C−H***O intramolecular hydrogen-bond.
Chem. – A Eur. J.  (2013), Vol. 19, 9908-9915.

5. M. Ramesh,  P. V. Bharatam, P. Venugopalan and R. Kishore
Importance of C−H***O intramolecular hydrogen-bonding across a non-proteinogenic γ-aminobenzoic acid residue: Stabilization of a flat β-strand-like template.
Cryst. Growth & Design, (2013), Vol. 13, 2004-2012.

6. R. Kaur, and R. Kishore 
Isostructural unsbranched alkyl-chains as tools for stabilizing β-turn structure. 
Biopolymers,  (2013), Vol. 99, 419-426.

7.M. M. Bhadbhade and R. Kishore
Intramolecular C−H***O hydrogen-bond mediated stabilization of a cis-DPro imide-bond in a stereocontrolled heterochiral model peptide
Biopolymers,  (2011), Vol. 97, 73-82.

8. N. Kumar, P. Venugopalan and R. Kishore
Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: Importance of a C−H***O interaction.
Biopolymers,  (2010), Vol. 94, 927-931.

9. N. Kumar and R. Kishore
Determination of an unusual secondary structural element in an immunostimulatin tetrapeptide rigin in aqueous environment: Insights via MD simulations, 1H NMR and CD spectroscopic studies
J. Pept. Sci., (2010), Vol. 16, 456-464.

10. S.-W. Ha, T. Asakura and R. Kishore
Distinctive influence of two hexafluoro solvents on the structural stabilization of Bombyx mori silk fibroin protein and its derived peptides: 13C NMR and CD studies.
Biomacromolecules, (2006), Vol. 7, 18-23.

11. A. K. Thakur and R. Kishore
Characterization of a β-turn and Asx-turns mimicry in a model peptide: Stabilization via C−H***O interaction.
Biopolymers, (2006), Vol. 81, 440-449.

12. A. K. Thakur and R. Kishore
Characterization of a β-turn and Asx-turns mimicry in a model peptide: Stabilization via C−H***O interaction.
Biopolymers, (2006), Vol. 81, 440-449.

13. T. Asakua, K. Ohgo, T. Ishida, P. Taddei, P. Monti and  R. Kishore
Possible implications of Ser and Tyr residues and intermolecular interactions on the appearance of silk I structure of Bombyx mori silk fibroin derived synthetic peptides: High-resolution 13C CP/MAS NMR study. 
Biomacromolecules, (2005), Vol. 6, 468-474.

14. R. Kishore
β-Ala containing peptides: Potentials in design and construction of bioactive peptides and protein secondary structure mimics. review article
Curr. Protein & Peptide Sci., (2004), Vol. 5, 435-455.

15.  J. Yao, K. Ohgo, R. Sugino, R. Kishore and T. Asakua                                                                      Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment using high-resolution solid-state 13C NMR spectroscopy.
Biomacromolecules, (2004), Vol. 5, 1763-1769

16. Mohan M. Bhadbhade and R. Kishore
An observation of non-superimposable stereogeometrical features in a non-chiral one-component β-Ala containing model peptide.
Biochem. Biophys. Res. Commun., (2004), Vol. 316, 1029-1036.

17. T. Gullion, R. Kishore and T. Asakura
Determination of dihedral angles and local structures in peptides by 13C-2H REDOR.
J. Am. Chem. Soc., (2003), Vol. 125, 7510-7511.

18. C. Zhao, J. Yao,  H. Masuda, R. Kishore and T. Asakura.
Structural characterization and artificial  fiber formation of Bombyx mori silk fibroin in hexafluoro-iso-propanol solvent system.
Biopolymers, (2003), Vol. 69, 253-259.

19. T. Asakura, H. Kato, J. Yao, R. Kishore and M. Shirai
Design, expression and structural characterization of hybrid proteins of Samia cynthia ricini and Bombyx mori silk fibroin.
Polymer J., (2002), Vol. 34, 936-943.

20. Ashish and R. Kishore
Folded conformation of an immunostimulating tetrapeptide rigin: High temperature molecular dynamics simulation study.
Bioorg. Med. Chem., (2002), Vol. 10, 4083-4090.

21. T. Asakura, R. Sugino, J. Yao, H. Takashima and R. Kishore
Comparative structure analysis of tyrosine and valine residues in unprocessed silk fibroin (Silk I) and in the processed silk fiber (Silk II) from Bombyx mori using solid-state 13C, 15N and 2H NMR.
Biochemistry, (2002), Vol. 41, 4415-4424.

22. A. K. Thakur and R. Kishore
Influence of hydrophobic interactions on the conformational adaptability of the β-Ala residue. 
J. Peptide Res., (2001), Vol. 57, 455-461.

23. A. K. Thakur and R. Kishore
Crystalllographic characterization of novel β-turn like folds in a model peptide: Stabilization by main-chain to side-chain interactions.
Tetrahedron Letter,  (2001), Vol. 42, 4691-4694.

24. A. K. Thakur, P. Venugopalan and R. Kishore
Collateral existence of a folded and an extended conformations of the β-Ala moiety in a model peptide.
Biochem. Biophys. Res. Commun., (2000), Vol. 273, 492-498.

25. A. K. Thakur, P. Venugopalan and R. Kishore
Entrapping unusual folding characteristics of the β-Ala Residues: Crystal and molecular struture of           Boc-β-Ala-Aib-β-Ala-NHCH3.
J. Peptide Res., (2000), Vol. 56, 55-58.

26. Ashish, A. Grover and R. Kishore
Characterisation of a novel type VII β-turn conformation for a bioactive tetrapeptide rigin: A synergy between theoretical and experimental results.
Eur. J. Biochem., (2000), Vol. 267, 1455-1463.

27. A. K. Thakur and R. Kishore
Stabilization of a novel β-turn like motif by non-conventional intramolecular hydrogen bonding interactions in a model peptide incorporating β-alanine.
Biopolymers, (2000), Vol. 53, 447-454.

28. Ashish, S. Banumathi, D. Velmurgan, Anushree and R. Kishore
Induced conformational preferences in a non-chiral beta-Ala residue: X-ray diffraction, 1H NMR, FT-IR and CD studies of Boc-β-Ala-D-Ala-NHCH3 and Boc-β-Ala-L-Ala-NHCH3.
Tetrahedron (1999), Vol. 55, 13791-13804.

29. A. K. Thakur, Ashish and R. Kishore
Novel hydrogen bonding ring motifs in a model peptide: crystal and molecular conformation.
Chem. Commun., (1999), 1643-1644.

30. V. Kothekar, Ashish, D. Gupta, and R. Kishore
Theoretical study of conformational flexibility of tuftsin in vacuum and in aqueous environment.
Ind. J. Biochem. Biophys., (1999), Vol. 36, 14-28.

31. S. Banumathi, D. Velmurugan, E. Subramanian, Ashish and R. Kishore
Acta Cryst. C, (1999), Vol. 55, 78-79.

32. A.K. Thakur and R. Kishore
An all-anti conformation of the β-Ala moiety in the crystalline state.
Tetrahedron Letters, (1999), Vol. 40, 5091-5094.

33. A. K. Thakur and R. Kishore
An observation of a folded beta-Ala conformation in a model peptide: Boc-L-Pip-β-Ala-NHCH3, X-ray diffraction study.
Tetrahedron Letters, (1998), Vol. 39, 9553-9556.

34. Ashish and R. Kishore
Thermodynamic characterizations of an intramolecularly hydrogen bonded C5-structure across proteinogenic residue.
FEBS Letters, (1997), Vol. 417, 97-100.

35. Ashish and R. Kishore
1H NMR spectroscopic signatures of an intraresidue hydrogen bonded C5-structure.
Tetrahedron Letters (1997), Vol. 38, 2767-2770.

36. R. Kishore
Identification of novel stereogeometrical features in β-Ala residue.
Tetrahedron Letters (1996), Vol. 37, 5747-5750.

37. K. Uma, R. Kishore and P. Balaram
Stereochemical constraints in peptide design: analysis of the influence of a disulphide bridge and an α-aminoisobutyryl residue on the conformation of a hexapeptide.
Biopolymers (1993), Vol. 33, 865-871.

38. R. Bardi, A. M. Piazzesi, M. Crisma, C. Toniolo and R. Kishore
Crystal Structure of N-tert-butyloxycarbonyl-β-alanyl-L-alanine methylamide,
Zeit. Kristallogr. (1993), Vol. 207, 290-292.

39. V. Pavone, B.D. Blasio, A. Lombardi, C. Isernia, C. Pedone, E. Benedetti, G. Valle, M. Crisma, C. Toniolo and R. Kishore
β-Alanine and β-bends. X-ray diffraction structure of three linear oligopeptides.
J. Chem. Soc. Perkin. Trans. (1992), Vol. 2, 1233-1237.

40. I. L. Karle, J. L. Flippen-Anderson, R. Kishore and P. Balaram
Cystine peptides: antiparallel β-sheet conformation of the cyclic biscystine peptide
Int. J. Peptide Protein Res. (1989), Vol. 34, 37-41.

41. I. L. Karle, R. Kishore, S. Raghothama and P. Balaram
Cyclic cystine peptides: Antiparallel β-sheet conformation for the 20-membered ring in                               Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe
        S ________________S
J. Am. Chem. Soc. (1988), Vol. 110, 1958-1963.

42. R. Kishore, S. Raghothama and P. Balaram
Synthetic peptide models for the redox-active disulfide loop of glutaredoxin conformational studies.
Biochemistry (1988), Vol. 27, 2462-2471.

43. R. Kishore, H. Ishizaki, Anthony T. Tu., A. Ravi and P. Balaram
Cystine peptides: Disulphide conformations in 14-membered loops investigated by Raman spectroscopy and circular dichroism.
Int. J. Peptide Protein Res. (1987), Vol. 30, 474-480.
44. S. Gaur, R. Kishore and G. P. Talwar
Synthetic vaccines in the making in research in industry.
Eds. Mulky, M.J., Srivastava, H.C. and B. Vatsaya, Oxford & IBH Publishing Co. Pvt. Ltd. (1987), pp. 126-139.

45. R. Kishore, S. Raghothama and P. Balaram
Cystine peptides.  The intramolecular antiparallel β-sheet conformation of a 20-membered cyclic peptide disulphide.
Biopolymers (1987), Vol. 26, 873-891.

46. R. Kishore, S. Raghothama and P. Balaram
Cystine peptides. Spectroscopic studies on the conformations of a cyclic pentapeptide disulphide.
Int. J. Peptide Protein Res. (1987), Vol. 29, 381-391.

47. R. Kishore and P. Balaram
Synthesis and conformational analysis of cyclic cystine peptides
J. Indian Institute of Science (1986), Vol. 66, 563-566.

48. R. Kishore and P. Balaram
Stereochemically constrained enkephalin analogs containing α-aminoisobutyric acid and 1-amino-cyclopentane-1-carboxylic acid in "Opioid Peptides : Medicinal Chemistry" Eds. R.S. Rapaka, G. Barnett & R.L. Hawks: National Institute of Drug Abuse (NIDA) Res. Monograph (1986), Vol. 69, 312-331.

49. R. Kishore and P. Balaram
Synthetic peptide models for active sites of disulfide-dithiols redox proteins in "Thioredoxin and Glutaredoxin Systems: Structure and Function." Proc. 9th Nobel Conference Eds. A. Holmgren, C.I. Braden, H. Jornvall and B.M. Sjoberg, Raven Press, New York, (1986), pp. 57-66.

50. R. Kishore, A. Kumar and P. Balaram
Cystine Peptides. The antiparallel β-sheet conformation of two synthetic cyclic Bis (cystine peptides).
J. Am. Chem. Soc. (1985), Vol. 107, 8019-8023.

51. R. Kishore and P. Balaram
Stabilization of γ-turn conformations in peptides by disulphide bridging.
Biopolymers (1985), Vol. 24, 2041-2043.

52.R. Kishore and P. Balaram
Cyclic biscystine peptides. Models for antiparallel β-sheet conformations.
J. Chem. Soc. Chem. Commun. (1984), Vol. 192, 778-779.

53. R. Kishore and P. Balaram
Synthesis & conformations of stereochemically restricted analogs of Leu5-enkephalinamide: Substitution of α-aminoisobutyric acid & 1-aminocyclopentane-1-carboxylic acid at positions 2 & 3.
Ind. J. Chem. (1984), Vol. 23 B, 1137-1144.

54. R.Kishore, M. K. Mathew and P. Balaram
A fluorescent peptide model for the thioredoxin active site.
FEBS Leters. (1983), Vol. 159, 221-224.


Present group members:

Mr. Vineet Kumar

Past group members:

Mr. Sameer K. Nath

Dr. Nigam Kumar

Dr. Ashwani K. Thakur

Dr. Ashish

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