Literature DB >> 18846198

Segment Coupling to a Highly Hindered N-Terminal, Alamethicin-Related alpha-Aminoisobutyric Acid (Aib) Residue.

Louis A Carpino1, Adel Ali Abdel-Maksoud, E M E Mansour, Mohamed A Zewail.   

Abstract

A model [6 + 5] segment coupling process involving a C-terminal valine hexapeptide acid and a resin-attached pentapeptide amide which N-terminated in a hindered Aib unit was examined using a variety of HOAt-derived coupling reagents. Best results were observed with HAPyU in DCM solvent in which loss of configuration amounted to 5.8%.

Entities:  

Year:  2007        PMID: 18846198      PMCID: PMC2344146          DOI: 10.1016/j.tetlet.2007.07.215

Source DB:  PubMed          Journal:  Tetrahedron Lett        ISSN: 0040-4039            Impact factor:   2.415


  3 in total

1.  Mechanistic studies of peptide oxazolone racemization.

Authors:  M Goodman; W J McGahren
Journal:  Tetrahedron       Date:  1967-05       Impact factor: 2.457

2.  Total synthesis in solution of alamethicin F50/5 by an easily tunable segment condensation approach.

Authors:  Cristina Peggion; Irene Coin; Claudio Toniolo
Journal:  Biopolymers       Date:  2004       Impact factor: 2.505

3.  Studies on asymmetric induction associated with the coupling of N-acylamino acids and N-benzyloxycarbonyldipeptides.

Authors:  N L Benoiton; Y C Lee; F M Chen
Journal:  Int J Pept Protein Res       Date:  1991-12
  3 in total
  1 in total

1.  Evolving the use of peptides as components of biomaterials.

Authors:  Joel H Collier; Tatiana Segura
Journal:  Biomaterials       Date:  2011-06       Impact factor: 12.479

  1 in total

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