Expedient synthesis of pseudo-Pro-containing peptides: towards constrained peptidomimetics and foldamers

Marco, Rossella De; Tolomelli, Alessandra; Campitiello, Marilena; Rubini, Pasqualina; Gentilucci, Luca

doi:10.1039/c2ob07172j

Cited by 23 publications

(13 citation statements)

References 91 publications

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“…Next, to determine the role of the N-terminal protecting group (Pg) in the formation of the cyclic urethane moiety, a model peptide Pg-ASF-Rink AM with other N-terminal protecting groups such as acetyl, tosyl, and Boc was investigated (entries 7–9, Table 2 ). Contrary to earlier studies, 24 the results indicated that the formation of the cyclic urethane moiety from serine by activating the backbone peptide chain is independent of the nature of the N-terminal protecting group.…”

Section: Resultscontrasting

confidence: 99%

Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

2017

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Section: Resultscontrasting

confidence: 99%

Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

2017

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“…Recently, we proposed the expedient cyclization of β‐hydroxy‐α‐amino acids already embedded in a oligopeptide sequence, by treatment with disuccinimidyldicarbonate (DSC) and a base, to give oxazolidinone‐peptides (Oxd) . Depending from the stereochemistry, linear peptides including two consecutive β‐hydroxy‐α‐amino acids gave rise to sequences Oxd‐Oxd or ΔAbu‐Oxd; these scaffolds adopted well‐defined extended or folded conformations, in particular normal or inverse β‐turns of type I or II (Scheme ) …”

Section: Introductionmentioning

confidence: 99%

5‐aminomethyloxazolidine‐2,4‐dione hybrid α/β‐dipeptide scaffolds as inductors of constrained conformations: Applications to the synthesis of integrin antagonists

et al. 2015

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Peptidomimetics represent an attractive starting point for drug discovery programs; in particular, peptidomimetics that result from the incorporation of a heterocycle may take advantage of increased enzymatic stability and higher ability to reproduce the bioactive conformations of the parent peptides, resulting in enhanced therapeutic potential. Herein, we present mimetics of the α4β1 integrin antagonist BIO1211 (MPUPA-Leu-Asp-Val-Pro-OH), containing a aminomethyloxazolidine-2,4-dione scaffold (Amo). Interestingly, the retro-sequences PhCOAsp(OH)-Amo-APUMP including either (S)- or (R)-configured Amo displayed significant ability to inhibit the adhesion of α4β1 integrin expressing cells, and remarkable stability in mouse serum. Possibly, the conformational bias exerted by the Amo scaffold determined the affinity for the receptors. These peptidomimetics could be of interest for the development of small-molecule agents effective against inflammatory processes and correlated autoimmune diseases.

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“…Earlier attempts of utilizing DSC for the formation of the cyclic urethane moiety on Fmoc/Boc peptides were unsuccessful and led to the formation of dehydroalanine. 23 Hydrolysis of the peptide bond at the cyclic urethane moiety (B) produces an N-terminal peptide fragment (C) and the cyclic urethane modified C-terminal fragment (D).…”

Section: Site-selective Chemical Cleavage Of Peptide Bonds †mentioning

confidence: 99%

Site-selective chemical cleavage of peptide bonds

Elashal

Raj

2016

Chem. Commun.

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Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid residues in the peptide chain and selectively cleave a peptide bond. Building on this principle, we have developed an approach that utilizes a chemical reagent to selectively modify the serine residue in a peptide chain and leads to the cleavage of a peptide backbone at the N-terminus of the serine residue. After cleavage, modified residues can be converted back to the original fragments. This method exhibits broad substrate scope and selectively cleaves various bioactive peptides with post-translational modifications (e.g. N-acetylation and -methylation) and mutations (d- and β-amino acids), which are a known cause of age related diseases.

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Expedient synthesis of pseudo-Pro-containing peptides: towards constrained peptidomimetics and foldamers

Cited by 23 publications

References 91 publications

Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

5‐aminomethyloxazolidine‐2,4‐dione hybrid α/β‐dipeptide scaffolds as inductors of constrained conformations: Applications to the synthesis of integrin antagonists

Site-selective chemical cleavage of peptide bonds

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