Dipeptidyl Peptidase (DPP)
Dipeptidyl Peptidase (DPP) — An enzyme that cleaves dipeptides from the N-terminus of polypeptides, with DPP-IV being a key degradation enzyme for incretin peptides like GLP-1.
What Is Dipeptidyl Peptidase?
Dipeptidyl peptidase IV (DPP-IV, DPP-4, CD26) is a serine exopeptidase that cleaves dipeptides from the N-terminus of peptides containing Pro or Ala at position 2 (X-Pro↓ or X-Ala↓). DPP-IV rapidly degrades GLP-1 and GIP (t1/2 ~2 min), making it a major target for diabetes drug design.
Significance
- DPP-IV inhibitors: Gliptins (sitagliptin, saxagliptin) are oral diabetes drugs that extend endogenous GLP-1 half-life
- DPP-IV-resistant analogs: Semaglutide, liraglutide contain Aib at position 2 to resist DPP-IV cleavage
- Peptide design: Avoid Pro/Ala at position 2 or use D-Ala to block DPP-IV degradation
Frequently Asked Questions
What is Dipeptidyl Peptidase (DPP)?
An enzyme that cleaves dipeptides from the N-terminus of polypeptides, with DPP-IV being a key degradation enzyme for incretin peptides like GLP-1.
Why is Dipeptidyl Peptidase (DPP) important in peptide research?
Dipeptidyl Peptidase (DPP) is a fundamental concept in biochemistry as it relates to peptide science. It directly influences experimental design, compound characterization, and the reliability of research outcomes across biochemistry and molecular biology disciplines.
Authority Sources
- Dipeptidyl Peptidase (DPP) on Wikipedia
- Search Dipeptidyl Peptidase (DPP) on PubChem (NIH)
- Research articles on ScienceDirect