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Cited by 102Proteoglycans and glycosaminoglycans researchPolymer Surface Interaction StudiesProtein Structure and Dynamics

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Design of Peptides with High Affinities for Heparin and Endothelial Cell Proteoglycans

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Verrecchio, Angela, Germann, Markus W., Schick, Barbara P., Kung, Brian, Twardowski, Thomas, San Antonio, James D.·2000·Journal of Biological Chemistry
DOI 10.1074/jbc.275.11.7701
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Abstract

Proteoglycan-binding peptides were designed based on consensus sequences in heparin-binding proteins: XBBXBX and XBBBXXBX, where X and B are hydropathic and basic residues, respectively. Initial peptide constructs included (AKKARA)(n) and (ARKKAAKA)(n) (n = 1-6). Affinity coelectrophoresis revealed that low M(r) peptides (600-1,300) had no affinities for low M(r) heparin, but higher M(r) peptides (2,000-3,500) exhibited significant affinities (K(d) congruent with 50-150 nM), which increased with peptide M(r). Affinity was strongest when sequence arrays were contiguous and alanines and arginines occupied hydropathic and basic positions, but inclusion of prolines was disruptive. A peptide including a single consensus sequence of the serglycin proteoglycan core protein bound heparin strongly (K(d) congruent with 200 nM), likely owing to dimerization through cysteine-cysteine linkages. Circular dichroism showed that high affinity heparin-binding peptides converted from a charged coil to an alpha-helix upon heparin addition, whereas weak heparin-binding peptides did not. Higher M(r) peptides exhibited high affinities for total endothelial cell proteoglycans (K(d) congruent with 300 nM), and approximately 4-fold weaker affinities for their free glycosaminoglycan chains. Thus, peptides including concatamers of heparin-binding consensus sequences may exhibit strong affinities for heparin and proteoglycans. Such peptides may be applicable in promoting cell-substratum adhesion or in the design of drugs targeted to proteoglycan-containing cell surfaces and extracellular matrices.

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Crossref · 10.1074/jbc.275.11.7701

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  1. Iozzo, 1985, Cancer Res., 45, 5677

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Metadata

Authors
Verrecchio, A., Germann, M. W., Schick, B. P., Kung, B., Twardowski, T., & San Antonio, J. D.
Affiliations
  • Thomas Jefferson University (US)
  • Drexel University (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-03
Volume
275
Issue
11
Pages
7701-7707
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.275.11.7701
OpenAlex
W2146240095
Cited by
102
References
42
Citations by year
2025: 2 · 2024: 5 · 2023: 5 · 2022: 3 · 2021: 3 · 2020: 4 · 2019: 3 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 4 · 2014: 2 · 2013: 5
FWCI
3.08
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01hl029282-15)
  • National Heart, Lung, and Blood Institute (HL29282, HL 53590)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
heparin-binding peptides, peptide binding affinity, peptide dimerization, alpha-helix formation, glycosaminoglycan chains, cell-substrate adhesion
MeSH terms
Amino Acid Sequence, Circular Dichroism, Endothelium, Vascular, Heparin, Humans, Molecular Sequence Data, Oligopeptides, Peptides, Protein Binding, Proteoglycans, Consensus Sequence

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