Conformational restriction of Tyr and Phe side chains in opioid peptides: Information about preferred and bioactive side‐chain topology-Reference-Cited by-同舟云学术

Conformational restriction of Tyr and Phe side chains in opioid peptides: Information about preferred and bioactive side‐chain topology

Published:1996-01 Issue:1 Volume:38 Page:1-12
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Tourwé Dirk¹,Verschueren Kris¹,Frycia Anne¹,Davis Peg²,Porreca Frank²,Hruby Victor J.²,Toth Geza²³,Jaspers Hendrika¹,Verheyden Patricia¹,Van Binst Georges¹

Affiliation:

1. Eenheid Organische Chemie, Vrije Universiteit Brussel, Pleinlaan 2, B‐1050 Brussels, Belgium

2. Department of Pharmacology, University of Arizona, Tucson, AZ, USA

3. Department of Chemistry, University of Arizona, Tucson, AZ, USA and Biological Research Center, Szeged, Hungary

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/%28SICI%291097-0282%28199601%2938%3A1%3C1%3A%3AAID-BIP1%3E3.0.CO%3B2-%23

Reference42 articles.

1. Conformational restrictions of biologically active peptides via amino acid side chain groups

2. Differential contribution of C-terminal regions of dermorphin and dermenkephalin to opioid-sites selection and binding potency

3. Function of negative charge in the "address domain" of deltorphins

4. Structure-Activity relationship of tetrapeptides related to dermorphin: A 500-MHz1H-nmr study

5. New insights on ?/? selectivity of opioid peptides: Conformational analysis of deltorphin analogues

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