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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

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Published on: August 20, 2018

N-Hydroxy peptides: solid-phase synthesis and β-sheet propensity.

Matthew P Sarnowski¹, Juan R Del Valle¹

¹Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, USA. jdelvalle@nd.edu.

Organic & Biomolecular Chemistry

|May 1, 2020

Summary

Introducing N-hydroxy peptides, this study details a solid-phase synthesis method. Backbone N-hydroxylation enhances beta-hairpin stability, offering new avenues for designing constrained peptidomimetics.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Published on: November 21, 2013

Area of Science:

Peptide chemistry and peptidomimetics.
Structural biology and biophysics.

Background:

Peptide backbone modifications significantly impact conformational and physicochemical properties.
Main-chain N-hydroxy groups in peptides, though uncommon, confer unique conformational preferences and biological activities.

Purpose of the Study:

To develop a versatile solid-phase synthesis method for N-hydroxy peptides.
To evaluate the effect of backbone N-hydroxylation on peptide secondary structure stability, specifically β-hairpin conformation.
To explore N-hydroxy-α-amino acids as analogs to α-hydrazino acids for β-sheet stabilization.

Main Methods:

Solid-phase synthesis of peptides incorporating N-hydroxy-α-amino acids.
Utilizing a model β-hairpin system to assess secondary structure stability.
Comparative analysis of N-hydroxy groups versus N-methyl substituents in the β-strand region.

Main Results:

A robust method for preparing N-hydroxy peptides on solid support was established.
Backbone N-hydroxy groups are well-tolerated within the β-strand of a β-hairpin without energetic penalty.
A di-N-hydroxylated peptide variant demonstrated enhanced β-hairpin stability.

Conclusions:

Backbone N-hydroxylation is a viable strategy for peptide modification.
N-hydroxy peptides can be readily synthesized and incorporated into secondary structures.
This approach provides a novel tool for designing conformationally constrained peptidomimetics with potential therapeutic applications.