Peptides with 6-Aminohexanoic Acid: Synthesis and Evaluation as Plasmin Inhibitors

Fifteen new peptide derivatives of ɛ-aminocaproic acid (EACA) containing the known fragment –Ala–Phe–Lys– with an affinity for plasmin were synthesised in the present study. The synthesis was carried out a solid phase. The following compounds were synthesised: H–Phe–Lys–EACA–X, H– d -Ala–Phe–Lys–EAC...

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Bibliographic Details
Published in:International journal of peptide research and therapeutics 2017-06, Vol.23 (2), p.235-245
Main Authors: Purwin, Maciej, Markowska, Agnieszka, Bruzgo, Irena, Rusak, Tomasz, Surażyński, Arkadiusz, Jaworowska, Urszula, Midura-Nowaczek, Krystyna
Format: Article
Language:English
Subjects:
Animal Anatomy
Biochemistry
Biomedical and Life Sciences
Biosynthesis
Histology
Life Sciences
Molecular Medicine
Morphology
Peptides
Pharmaceutical Sciences/Technology
Pharmacology/Toxicology
Polymer Sciences
Proteases
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Summary:Fifteen new peptide derivatives of ɛ-aminocaproic acid (EACA) containing the known fragment –Ala–Phe–Lys– with an affinity for plasmin were synthesised in the present study. The synthesis was carried out a solid phase. The following compounds were synthesised: H–Phe–Lys–EACA–X, H– d -Ala–Phe–Lys–EACA–X, H–Ala–Phe–Lys–EACA–X, H– d -Ala–Phe–EACA–X and H–Ala–Phe–EACA–X, where X = OH, NH 2 and NH–(CH 2 ) 5 –NH 2 . All peptides, except for those containing the sequence H–Ala–Phe–EACA–X, displayed higher inhibitory activity against plasmin than EACA. The most active and selective inhibitor of plasmin was the compound H– d -Ala–Phe–Lys–EACA–NH 2 which inhibited the amidolytic activity of plasmin (IC 50  = 0.02 mM), with the antifibrinolytic activity weaker than EACA. The resulting peptides did not affect the viability of fibroblast cells, colon cancer cell line DL D -1, breast MCF-7 and MDA-MB-231 cell lines.
ISSN:1573-3149
1573-3904
DOI:10.1007/s10989-016-9555-3