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• W3127267738 abstract "This thesis entitled “Design and Synthesis of Peptidomimics Constrained in Helical and Sheet Conformations Using a Novel Covalent Surrogate for the Peptide Main Chain Hydrogen Bond” is divided into six chapters.Chapter 1: Introduction to Ordered Conformations of Peptides and Strategies for Constraining Short Peptides in Ordered Conformations.The first chapter describes the different types of protein secondary structures and introduces the various prominent strategies developed thus far to constrain short peptides in ordered secondary structure-like conformations, with specific emphasis on helical and parallel β-sheet folds.Chapter 2: Design of Structure and General Methodology for the synthesis of Novel H-Bond Surrogate Constrained Cyclic α-Helical MimicsHere we develop the first design of the propyl linker as a covalent surrogate for the peptide H-bond. The first synthetic methodology is described for the synthesis of constraining shortest peptide sequences (tripeptides) in α-helix-like conformations. The Macrolactamization strategy proved to work best as the final step for cyclization. All residues of the turn are completely retained in the constrained sequence, unlike any other earlier method. More importantly, there are no metal involved as catalysts in any of the synthetic transformations, hence removing the problem of metal-bound cyclic structures – which have otherwise rendered these structures non-usable as drug leads in the earlier models. Gly-rich peptides have been constrained as extreme cases of highest chain entropy and least helix propensity. Both secondary and tertiary amide containing peptides have been synthesized using this protocol. Note that the macrolactamization was found to be better than the Fukuyama-Mitsunobu N-alkylation protocol for the final cyclization step. Chapter 3: Synthesis of C-terminal Extended HBS-Constrained Helical Turn Mimics – Validation of the Versatility of Current synthetic protocol The developed cyclization protocol is extended towards the synthesis of C-terminalextended α-helical turn mimics using a solution phase peptide synthesis procedure. Peptides which extend belong the helical turn by a high entropy Gly-residue at the C-terminal are synthesized. The versatility of the synthetic methodology to accommodate sterically constrained amino acid residues – in the form of phenylalanine residue – at any of the positions i+1, i+2 or i+3 of the constrained helical turn is demonstrated. The synthesized are easily isolated withoutneed for column chromatography, in high purity and good yields – this is due to the presence of the N-terminal amino group, salts of which are easily triturated to remove all other organic impurities.Chapter 4: Synthesis and CD conformational analyses of HBS constrained α-Helical turn mimics containing residues with improved helical propensities Alanine residue has the highest helix propensity among all other natural α-amino acid residues. Its enthalpic contribution to the helical conformation is 1 kcal/mol more than that for the Glyresidue,…" @default.
• W3127267738 created "2021-02-15" @default.
• W3127267738 creator A5081516011 @default.
• W3127267738 date "2018-01-01" @default.
• W3127267738 modified "2023-09-23" @default.
• W3127267738 title "Design and Synthesis of Peptidomimics Constrained in Helical and Sheet Conformations using a Novel Covalent Surrogate for the Peptide Main Chain Hydrogen Bond" @default.
• W3127267738 hasPublicationYear "2018" @default.
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