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Enzymatic Modification of Self-Assembled Peptide Structures with Tissue Transglutaminase

Collier, Joel H., Messersmith, Phillip B.·2003·Bioconjugate Chemistry

Abstract

A de novo peptide that self-assembles into fibrillar structures and serves as a substrate for the cross-linking enzyme tissue transglutaminase was developed (Ac-QQKFQFQFEQQ-Am). Congo red staining, circular dichroism, and FTIR spectroscopy showed that this 11-amino acid peptide produced predominantly beta-sheet structures. TEM with negative staining and quick-freeze deep etch (QFDE) TEM showed that the peptide structures were composed of a highly entangled fibrillar network. These beta-sheet fibrillar nanostructures were then covalently coupled to pendant amine-containing biomolecules via tissue transglutaminase. MALDI-TOF mass spectrometry and HPLC were utilized to monitor the extent of the transglutaminase modification of the peptide, showing that as many as five glutamines in the peptide were reactive via transglutaminase for covalent conjugation. This strategy, based on the post-assembly modification of a self-assembling peptide, has potential applications for tailoring supramolecular structures for drug delivery, tissue engineering, or other biomedical applications.

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Metadata

Authors
Collier, J. H., & Messersmith, P. B.
Venue
Bioconjugate Chemistry
Published
2003-06-24
Volume
14
Issue
4
Pages
748-755
ISSN
  • 1043-1802 (ISSN-L)
  • 1520-4812
OpenAlex
W2161417492
Cited by
171
References
0
FWCI
1.93
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Enzymatic Modification of Self-Assembled Peptide Structures with Tissue Transglutaminase. https://app.cochat.ai/papers/10.1021/bc034017t
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Collier, J. H., & Messersmith, P. B. (2003). Enzymatic Modification of Self-Assembled Peptide Structures with Tissue Transglutaminase. Bioconjugate Chemistry. https://doi.org/10.1021/bc034017t

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