Sulfo-Cy7.5-GPLGVRGC MMP-Responsive Peptide

Sulfo-Cy7.5-GPLGVRGC MMP-Responsive Peptide uses the published matrix-metalloproteinase-responsive peptide GPLGVRGC. The related GPLGVR motif is a widely used substrate sequence for MMP-responsive imaging, drug-delivery, and biomaterial systems.

MMP-Responsive Peptide Substrate

Matrix metalloproteinases are zinc-dependent extracellular proteases that remodel extracellular matrix proteins. Increased MMP activity is studied in cancer, inflammation, tissue remodeling, and wound-healing systems. Short MMP-cleavable peptides provide convenient substrates for constructing activatable probes and enzyme-responsive linkers.

Published work directly tested GPLGVRGC cleavage with activated human MMP-2 and used the peptide to construct PEG-peptide conjugates and activatable nanoparticle systems. The cysteine at the C-terminus provides a convenient thiol for conjugation while the GPLGVR region contains the protease-sensitive element.

Sulfo-Cy7.5 Fluorescent Reporter

LT8679 includes an N-terminal Sulfo-Cy7.5 label and C-terminal amidation. Sulfonated near-infrared dyes are useful in optical imaging research because their long-wavelength excitation/emission can reduce interference from many visible-range cellular fluorophores.

Research Applications

• MMP-2/MMP-9 substrate assays
• Protease-activated imaging probes
• Enzyme-responsive nanoparticle systems
• Hydrogel and biomaterial cleavage studies
• Protease kinetics
• Near-infrared fluorescence studies

References

Lee H, et al. Polydopamine-based surface modification for the development of peritumorally activatable nanoparticles. Pharm Res. 2013.
Public source / publication

Chuang CH, et al. In vivo positron emission tomography imaging of protease activity by generation of a hydrophobic product from a noninhibitory protease substrate. Clin Cancer Res. 2012.
Public source / publication

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Research Use Only. Not for human, diagnostic, clinical, or therapeutic use.

Sulfo-Cy7.5-GPLGVRGC MMP-Responsive Peptide is a 8-residue synthetic peptide with the sequence Gly-Pro-Leu-Gly-Val-Arg-Gly-Cys. Cy7 provides a near-infrared fluorescent label. The sequence contains 1 cysteine residue, providing potential thiol/disulfide chemistry when the thiol is available; is Gly/Pro-rich, a composition that can influence local backbone flexibility. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence.

• fluorescence-based detection
• binding or localization assay development
• thiol-selective conjugation or immobilization studies
• LC-MS/HPLC analytical method development
• sequence-specific assay controls

Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions.