FA-Leu-Gly-Pro-Ala-OH TFA 

FA-Leu-Gly-Pro-Ala-OH TFA is a furylacryloyl-terminal tetrapeptide that serves as a substrate for bacterial collagenase and spirochete metalloendopeptidase. FA-Leu-Gly-Pro-Ala-OH TFA is specifically hydrolyzed by spirochete collagenase only at the Leu-Gly bond. FA-Leu-Gly-Pro-Ala-OH TFA can be used to determine the equilibrium constant of peptide bond hydrolysis, and also to detect collagenase-mediated cleavage reactions via turbidimetry based on absorbance reduction^[1][2].

FA-Leu-Gly-Pro-Ala-OH (1 mM Ca²⁺; no added Ca²⁺) TFA is hydrolyzed at the Leu-Gly bond by the partially purified metalloendopeptidase from unspeciated treponeme strain US with near-identical activity in the presence of 1 mM Ca²⁺ or without added Ca^2+[1].
FA-Leu-Gly-Pro-Ala-OH (5 mM; 15 min) TFA was not cleaved by crude nematocyst extract from Velella velella, which did not exhibit detectable collagenase activity against the substrate under the tested conditions^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

590.55

C₂₅H₃₃F₃N₄O₉

FA-Leu-Gly-Pro-Ala

FA-LGPA

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Mäkinen K K, et al. Hydrolysis of the Leu-Gly bond of phenylazobenzyl-oxycarbonyl-l-Pro-l-Leu-Gly-l-Pro-D-Arg (a substrate of microbial collagenases) by treponemes isolated from the subgingival plaque of periodontitis patients[J]. Current Microbiology, 1990, 20(1): 69-74.

  [2]. Tassara E, et al. Proteomic Analysis and Biochemical Characterization of the Nematocyst Extract of the Hydrozoan Velella velella. Mar Drugs. 2024 Oct 12;22(10):468.  [Content Brief]