Tripeptides with non-code amino acids as potential serine proteases inhibitors

Markowska, Agnieszka; Bruzgo, Magdalena; Surażyński, Arkadiusz; Midura-Nowaczek, Krystyna

doi:10.3109/14756366.2011.651463

Cited by 3 publications

(2 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In a similar our paper on the inhibition of plasmin and urokinase, the effect of amino acid substitution on a known inhibitor of similar sequence was described. In place of alanine in the sequence Ser-Ala-Arg other aliphatic [56] or aromatic [57] amino acids were introduced. In homoleucine and neoglycine, there was a loss of enzymes inhibition, but selectivity was found for α-methylalanine and α-aminobutanoic acid.…”

Section: Discussionmentioning

confidence: 99%

The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity

et al. 2019

Self Cite

View full text Add to dashboard Cite

KTTKS is a matrikine that originates from the proteolytic hydrolysis of collagen. This peptide stimulates ECM production and types I and III collagen expression in vitro. A more stable form of KTTKS is pal-KTTKS, known as Matrixyl® or palmitoyl pentapeptide-3. A series of novel pentapeptides, analogues of KTTKS with the general formula X-KTTKS-OH(NH2), where X = acetyl, lipoyl, palmitoyl residues, was designed and synthesized. Their effect on amidolytic activity of urokinase, thrombin, trypsin, plasmin, t-PA, and kallikrein were tested. Cytotoxic tests on fibroblasts, as well as collagen and DNA biosynthesis tests for selected peptides, were also carried out. The test results showed that the most active plasmin inhibitors were palmitoyl peptides, whether in acid or amide form. No biological effects of lysine modification to arginine in the synthesized peptides were found. None of the synthesized peptides was not cytotoxic on fibroblasts, and three of them showed cell growth. These three compounds showed no concentration-activity relationship in the collagen and DNA biosynthesis assays.

show abstract

Section: Discussionmentioning

confidence: 99%

The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

“…MCF-7, MDA-MB-231 and DLD cells were maintained as described above. The detailed description of the method is given by (Markowska et al 2013 ).…”

Section: Methodsmentioning

confidence: 99%

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

Purwin

Markowska

Bruzgo

et al. 2016

Int J Pept Res Ther

Self Cite

View full text Add to dashboard Cite

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, NH2 and NH–(CH2)5–NH2. 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–NH2 which inhibited the amidolytic activity of plasmin (IC50 = 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 DLD-1, breast MCF-7 and MDA-MB-231 cell lines.

show abstract

Synthesis and Biological Activity of N-Sulfonyltripeptides with C-Terminal Arginine as Potential Serine Proteases Inhibitors

Markowska

Bruzgo

Gorodkiewicz

et al. 2012

Int J Pept Res Ther

Self Cite

View full text Add to dashboard Cite

Tripeptides of the general X-SO2-d-Ser-AA-Arg-CO-Y formula, where X = α-tolyl, p-tolyl, 2,4,6-triisopropylphenyl; AA = alanine, glycine, norvaline and Y = OH, NH-(CH2)5NH2 were obtained and tested for their effect on the amidolytic activities of urokinase, thrombin, trypsin, plasmin, t-PA and kallikrein. The most active compound towards urokinase was PhCH2SO2-d-Ser-Gly-Arg-OH with Ki value 5.4 μM and the most active compound toward thrombin was PhCH2SO2-d-Ser-NVa-Arg-OH with Ki value 0.82 μM. The peptides were nontoxic against porcine erythrocytes in vitro. PhCH2SO2-d-Ser-Gly-Arg-OH showed cytotoxic effect against DLD cell lines with IC50 values of 5 μM. For the highly selective determination of the interaction of some of the synthesised acids of tripeptides with urokinase and plasmin the Surface Plasmon Resonance Imaging sensor has been applied. These compounds bind to urokinase and plasmin in 0.05 mM concentration.

show abstract

Tripeptides with non-code amino acids as potential serine proteases inhibitors

Cited by 3 publications

References 25 publications

The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity

The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity

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

Synthesis and Biological Activity of N-Sulfonyltripeptides with C-Terminal Arginine as Potential Serine Proteases Inhibitors

Contact Info

Product

Resources

About