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

Verrecchio, Angela; Germann, Markus W.; Schick, Barbara P.; Kung, Brian; Twardowski, Thomas; San Antonio, James D.

doi:10.1074/jbc.275.11.7701

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

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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Multiple binding sites of apoE molecules increase GAG binding.
“This notion that multiple binding sites of apoE molecules increase the GAG binding is consistent with the previous study of peptides including heparin binding consensus sequences showing that multiple copies of the heparin binding site enhance the binding affinity through cooperativity effects (51).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [51]

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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: Germann, Markus W.
Twardowski, Thomas
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: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7526 d)
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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Design of Peptides with High Affinities for Heparin and Endothelial Cell Proteoglycans

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