Reactive Intermediates in Peptide Synthesis:  First Crystal Structures andab InitioCalculations of 2-Alkoxy-5(4H)-oxazolones from Urethane-Protected Amino Acids

1997 ◽  
Vol 119 (18) ◽  
pp. 4136-4142 ◽  
Author(s):  
Marco Crisma ◽  
Giovanni Valle ◽  
Fernando Formaggio ◽  
Claudio Toniolo ◽  
Alessandro Bagno
Keyword(s):  
Amino Acids ◽  
Crystal Structures ◽  
Peptide Synthesis ◽  
Reactive Intermediates

scholarly journals One-Pot Ring-Opening Peptide Synthesis Using α,α-Difluoro-β-Lactams

Synthesis ◽  
2020 ◽  
Vol 52 (23) ◽  
pp. 3657-3666 ◽  
Author(s):  
Masaaki Omote ◽  
Atsushi Tarui ◽  
Masakazu Ueo ◽  
Marino Morikawa ◽  
Masahiko Tsuta ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Methyl Ester ◽  
Peptide Synthesis ◽  
Ring Opening ◽  
Reactive Intermediates ◽  
One Pot ◽  
Open Chain ◽  
Lactam Ring

α,α-Difluoro-β-lactams successfully underwent ring-opening aminolysis with various amino acids in 2,2,2-trifluoroethanol to afford fluorine-containing peptides. In this aminolysis, it was found that 2,2,2-trifluoroethanol first attacked the α,α-difluoro-β-lactams with cleavage of lactam ring to form the corresponding open-chain 2,2,2-trifluoroethyl esters as reactive intermediates. The trifluoroethyl esters were more electrophilic compared with the corresponding methyl ester and thereby accelerated the aminolysis with various amino acids to form β-amino acid peptides with α,α-difluoromethylene unit.

The dependence of racemization in peptide synthesis on the relative configuration of amino acids

1978 ◽  
Vol 19 (30) ◽  
pp. 2711-2712 ◽  
Author(s):  
Anatol Arendt ◽  
Aleksander M. Kołodziejczyk ◽  
Teresa Sołowska
Keyword(s):  
Amino Acids ◽  
Peptide Synthesis ◽  
Relative Configuration

scholarly journals Structural basis of adhesive binding by desmocollins and desmogleins

2016 ◽  
Vol 113 (26) ◽  
pp. 7160-7165 ◽  
Author(s):  
Oliver J. Harrison ◽  
Julia Brasch ◽  
Gorka Lasso ◽  
Phinikoula S. Katsamba ◽  
Goran Ahlsen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Crystal Structures ◽  
Structural Basis ◽  
Cellular Interactions ◽  
Opposite Charge ◽  
Charged Amino Acids ◽  
Structural Framework ◽  
Classical Cadherins ◽  
Coated Bead

Desmosomes are intercellular adhesive junctions that impart strength to vertebrate tissues. Their dense, ordered intercellular attachments are formed by desmogleins (Dsgs) and desmocollins (Dscs), but the nature of trans-cellular interactions between these specialized cadherins is unclear. Here, using solution biophysics and coated-bead aggregation experiments, we demonstrate family-wise heterophilic specificity: All Dsgs form adhesive dimers with all Dscs, with affinities characteristic of each Dsg:Dsc pair. Crystal structures of ectodomains from Dsg2 and Dsg3 and from Dsc1 and Dsc2 show binding through a strand-swap mechanism similar to that of homophilic classical cadherins. However, conserved charged amino acids inhibit Dsg:Dsg and Dsc:Dsc interactions by same-charge repulsion and promote heterophilic Dsg:Dsc interactions through opposite-charge attraction. These findings show that Dsg:Dsc heterodimers represent the fundamental adhesive unit of desmosomes and provide a structural framework for understanding desmosome assembly.

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