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Structural specificity of mucosal-cell transport and metabolism of peptide drugs: implication for oral peptide drug deliveryThe brush border membrane of intestinal mucosal cells contains a peptide carrier system with rather broad substrate specificity and various endo- and exopeptidase activities. Small peptide (di-/tripeptide)-type drugs with or without an N-terminal alpha-amino group, including beta-lactam antibiotics and angiotensin-converting enzyme (ACE) inhibitors, are transported by the peptide transporter. Polypeptide drugs are hydrolyzed by brush border membrane proteolytic enzymes to di-/tripeptides and amino acids. Therefore, while the intestinal brush border membrane has a carrier system facilitating the absorption of di-/tripeptide drugs, it is a major barrier limiting oral availability of polypeptide drugs. In this paper, the specificity of peptide transport and metabolism in the intestinal brush border membrane is reviewed.
Document ID
20050000634
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Bai, J. P.
(University of Minnesota, College of Pharmacy Minneapolis 55455)
Amidon, G. L.
Date Acquired
August 22, 2013
Publication Date
August 1, 1992
Publication Information
Publication: Pharmaceutical research
Volume: 9
Issue: 8
ISSN: 0724-8741
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Review, Tutorial
Review
Non-NASA Center
NASA Discipline Regulatory Physiology

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