Effect of a <i>cis</i>-4-aminopiperidine-3-carboxylic acid (<i>cis</i>-APiC) residue on mixed-helical folding of unnatural peptides

Choi, Sunglim; Shim, Jihyun; Kang, Philjae; Choi, Soo Hyuk

doi:10.1039/d1ob02223g

Cited by 1 publication

(2 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gellman and colleagues used γ-amino-β-prolines as foldamer building blocks and observed the same propensity to form a 12-helix as its carbocyclic analog without interaction of the ring nitrogen atom with the backbone 52 . The related cis -4-aminopiperidine-3-carboxylic acid ( cis -APiC) also forms a helical 12/10-folding as demonstrated by Choi et al 53 . These examples teach that a single additional heteroatom may not be sufficient for new hydrogen bond networks.…”

Section: Introductionmentioning

confidence: 89%

“…Interestingly, they are characterized by a large share of charged and hydrophilic amino acids capable of forming hydrogen bond networks 56 . Nevertheless, it has been observed that most non-natural foldamer types adopt relatively rigid structures in nonpolar solvents 35 , 43 , 44 , while their tendency for folding in aqueous environments is rather rare 33 , 34 , 50 – 53 .…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides

Just,

Palivec,

Bártová

et al. 2024

Commun Chem

View full text Add to dashboard Cite

Peptide-like foldamers controlled by normal amide backbone hydrogen bonding have been extensively studied, and their folding patterns largely rely on configurational and conformational constraints induced by the steric properties of backbone substituents at appropriate positions. In contrast, opportunities to influence peptide secondary structure by functional groups forming individual hydrogen bond networks have not received much attention. Here, peptide-like foldamers consisting of alternating α,β,γ-triamino acids 3-amino-4-(aminomethyl)-2-methylpyrrolidine-3-carboxylate (AAMP) and natural amino acids glycine and alanine are reported, which were obtained by solution phase peptide synthesis. They form ordered secondary structures, which are dominated by a three-dimensional bridged triazaspiranoid-like hydrogen bond network involving the non-backbone amino groups, the backbone amide hydrogen bonds, and the relative configuration of the α,β,γ-triamino and α-amino acid building blocks. This additional stabilization leads to folding in both nonpolar organic as well as in aqueous environments. The three-dimensional arrangement of the individual foldamers is supported by X-ray crystallography, NMR spectroscopy, chiroptical methods, and molecular dynamics simulations.

show abstract

Section: Introductionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides

Just,

Palivec,

Bártová

et al. 2024

Commun Chem

View full text Add to dashboard Cite

show abstract

Effect of a cis-4-aminopiperidine-3-carboxylic acid (cis-APiC) residue on mixed-helical folding of unnatural peptides

Abstract: The α/β-peptide 11/9-helix and the β-peptide 12/10-helix belong to “mixed” helices, in which two types of hydrogen bonds with opposite directionality alternate along the helical axis. cis-2-Aminocyclohaxanecarboxylic acid (cis-ACHC) is...

Cited by 1 publication

References 20 publications

Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides

Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides

Contact Info

Product

Resources

About