A Short Helix Formed by Cyclic β<sup>2,3</sup>‐Aminoxy Peptides in Protic Solvents

Yu, Hao; An, Ke; Zhang, Dan‐Wei; Yang, Dan

doi:10.1002/asia.201500338

Cited by 3 publications

References 42 publications

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Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

et al. 2019

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Nα‐acylated β2,3‐3‐azapeptides, or α‐hydrazidopeptides, of different lengths were synthesized starting from a conformationally restricted imidazolidinone‐tethered monomer. The preferential conformations of the oligomers were investigated by NMR and CD spectroscopy, supported by computational analysis. The experimental data clearly confirmed the tendency of these α‐hydrazidopeptides to fold into a zig‐zag (Z8) 8‐helix conformation, whose stability is length‐dependent, stabilized by the C=O(i)···H–N(i + 2) and N(i)···H–N(i + 1) intramolecular H‐bonding pattern, as well as by non‐standard C=O···H‐C hydrogen bonds.

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Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

et al. 2019

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Design Principles of Peptide Based Self-Assembled Nanomaterials

Seoudi

Mechler

2017

Peptides and Peptide-Based Biomaterials and Their Biomedical Applications

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The ability to design functionalized peptide nanostructures for specific applications is tied to the ability of controlling the morphologies of the self-assembled superstructures. That, in turn, is based on a thorough understanding of the structural and environmental factors affecting self-assembly. The aim of designing self-assembling nanostructures of controlled geometries is achieved via a combination of directional and non-directional second order interactions. If the interactions are distributed in a geometrically defined way, a specific and selective supramolecular self-assembly motif is the result. In this chapter we detail the role of non-covalent interactions on the self-assembly of peptides; we will also discuss different types of peptide building blocks and design rules for engineering unnatural supramolecular structures.

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Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

et al. 2018

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Antimicrobial peptides (AMPs) are short cationic peptides with a high affinity for membranes and emerged as a promising therapeutic approach with potential for treating infectious diseases. Chemical stabilization of short peptides proved to be a successful approach for enhancing their bio-physical properties. Herein, we designed and synthesized a panel of conformationally constrained antimicrobial peptides with either α-helical or β-hairpin conformation using templating strategies. These synthetic short constrained peptides possess different topological distributions of hydrophobic and hydrophilic residues and displayed distinct antimicrobial activity. Notably, the conformationally constrained α-helical peptides displayed a faster internalization into the bacteria cells compared to their β-hairpin analogues. These synthetic short constrained peptides showed killing effects on a broad spectrum of microorganisms mainly through pore formation and membrane damage which provided a potentially promising skeleton for the next generation of stabilized antimicrobial peptides.

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A Short Helix Formed by Cyclic β^2,3‐Aminoxy Peptides in Protic Solvents

Cited by 3 publications

References 42 publications

Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

Design Principles of Peptide Based Self-Assembled Nanomaterials

Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

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A Short Helix Formed by Cyclic β2,3‐Aminoxy Peptides in Protic Solvents

Cited by 3 publications

References 42 publications

Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

Imidazolidinone‐Tethered α‐Hydrazidopeptides – Synthesis and Conformational Investigation

Design Principles of Peptide Based Self-Assembled Nanomaterials

Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

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Product

Resources

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A Short Helix Formed by Cyclic β^2,3‐Aminoxy Peptides in Protic Solvents