Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery.
albumin
peptide chemical synthesis
peptide conformation
peptide interaction
peptides
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
21 08 2020
21 08 2020
Historique:
received:
08
05
2020
revised:
09
07
2020
pubmed:
11
7
2020
medline:
20
1
2021
entrez:
11
7
2020
Statut:
ppublish
Résumé
Rapid clearance by renal filtration is a major impediment to the translation of small bioactive biologics into drugs. To extend serum
Identifiants
pubmed: 32647013
pii: S0021-9258(17)50074-5
doi: 10.1074/jbc.RA120.014168
pmc: PMC7443490
pii:
doi:
Substances chimiques
Drug Carriers
0
Serum Albumin, Human
ZIF514RVZR
Banques de données
PDB
['1TF0', '4NE9']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12143-12152Informations de copyright
© 2020 Wang et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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