scholarly journals Comparative Study of the Chemical Reactivity of Helical Peptide Models for Protein Glycation

2017 ◽  
Vol 05 (02) ◽  
pp. 65-73
Author(s):  
Juan Frau ◽  
Daniel Glossman-Mitnik
Keyword(s):  
Comparative Study ◽  
Chemical Reactivity ◽  
Protein Glycation ◽  
Helical Peptide ◽  
Peptide Models

scholarly journals Hydrolysis, polarity, and conformational impact of C-terminal partially fluorinated ethyl esters in peptide models

2017 ◽  
Vol 13 ◽  
pp. 2442-2457 ◽  
Author(s):  
Vladimir Kubyshkin ◽  
Nediljko Budisa
Keyword(s):  
Chemical Reactivity ◽  
Hydrolytic Stability ◽  
Ethyl Esters ◽  
Peptide Sequence ◽  
Molecular Scaffolds ◽  
Biologically Relevant ◽  
C Terminus ◽  
Ester Moiety ◽  
Peptide Models ◽  
Ph Range

Fluorinated moieties are highly valuable to chemists due to the sensitive NMR detectability of the 19F nucleus. Fluorination of molecular scaffolds can also selectively influence a molecule’s polarity, conformational preferences and chemical reactivity, properties that can be exploited for various chemical applications. A powerful route for incorporating fluorine atoms in biomolecules is last-stage fluorination of peptide scaffolds. One of these methods involves esterification of the C-terminus of peptides using a diazomethane species. Here, we provide an investigation of the physicochemical consequences of peptide esterification with partially fluorinated ethyl groups. Derivatives of N-acetylproline are used to model the effects of fluorination on the lipophilicity, hydrolytic stability and on conformational properties. The conformational impact of the 2,2-difluoromethyl ester on several neutral and charged oligopeptides was also investigated. Our results demonstrate that partially fluorinated esters undergo variable hydrolysis in biologically relevant buffers. The hydrolytic stability can be tailored over a broad pH range by varying the number of fluorine atoms in the ester moiety or by introducing adjacent charges in the peptide sequence.

Reduction chemistry of hexagonal boron nitride sheets and graphene: a comparative study on the effect of alkali atom doping on their chemical reactivity

2020 ◽  
Vol 44 (15) ◽  
pp. 5725-5730
Author(s):  
Pablo A. Denis ◽  
Saif Ullah ◽  
Federico Iribarne
Keyword(s):  
Boron Nitride ◽  
Comparative Study ◽  
Hexagonal Boron Nitride ◽  
Chemical Reactivity ◽  
Alkali Atom

Functionalization of 2D BN dramatically increases the charge donated by lithium and 2D BN is no longer inert!

scholarly journals MMP-12 Catalytic Domain Recognizes Triple Helical Peptide Models of Collagen V with Exosites and High Activity

2008 ◽  
Vol 283 (31) ◽  
pp. 21779-21788 ◽  
Author(s):  
Rajagopalan Bhaskaran ◽  
Mark O. Palmier ◽  
Janelle L. Lauer-Fields ◽  
Gregg B. Fields ◽  
Steven R. Van Doren
Keyword(s):  
High Activity ◽  
Catalytic Domain ◽  
Helical Peptide ◽  
Peptide Models

A comparative study of the chemical reactivity of pyridoxamine, Ac-Phe-Lys and Ac-Cys with various glycating carbonyl compounds

Amino Acids ◽  
2008 ◽  
Vol 36 (3) ◽  
pp. 437-448 ◽  
Author(s):  
Miquel Adrover ◽  
Bartolomé Vilanova ◽  
Juan Frau ◽  
Francisco Muñoz ◽  
Josefa Donoso
Keyword(s):  
Comparative Study ◽  
Carbonyl Compounds ◽  
Chemical Reactivity

scholarly journals A Comparative Study of Ferulic Acid on Different Monosaccharide-Mediated Protein Glycation and Oxidative Damage in Bovine Serum Albumin

Molecules ◽  
2013 ◽  
Vol 18 (11) ◽  
pp. 13886-13903 ◽  
Author(s):  
Weerachat Sompong ◽  
Aramsri Meeprom ◽  
Henrique Cheng ◽  
Sirichai Adisakwattana
Keyword(s):  
Bovine Serum Albumin ◽  
Oxidative Damage ◽  
Comparative Study ◽  
Serum Albumin ◽  
Ferulic Acid ◽  
Bovine Serum ◽  
Protein Glycation
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