High impact information on Malformins

• Malformin A prevents IL-1 induced endothelial changes by inhibition of protein synthesis [1].
• These observations demonstrate that malformin-A1 recognizes and blocks IL1 beta binding to its receptor sites on monocytes and endothelial cells and protects these cells from IL1-induced procoagulant changes [2].
• Malformin-A1 inhibits the binding of interleukin-1 beta (IL1 beta) and suppresses the expression of tissue factor in human endothelial cells and monocytes [2].
• Malformin-A1, a cyclic pentapeptide of microbial origin, antagonized in a competitive manner the binding of 125I-IL1 beta (interleukin-1 beta) to human monocytes and cultured human umbilical vein endothelial cells (HUVEC) with IC50 values (doses which reduce specific binding by 50%) of 250 +/- 80 and 230 +/- 25 nM, respectively (N = 3) [2].
• Enhancement of fibrinolytic activity of U937 cells by malformin A1 [3].

Anatomical context of Malformins

• We have found that malformin A1, a cyclopentapeptide metabolite of Aspergillus niger, enhanced 2.0- to 3.2-fold the 125I-fibrin clot lysis when incubated at 1 to approximately 10 microM with both U937 cells and blood plasma, both of which were essential to the malformin A1 action [3].

Associations of Malformins with other chemical compounds

• Allomalformin is identical to the parent microbial peptide (malformin A, or briefly malformin) with respect to biological activity and conformation (ORD and CD spectra) and is indistinguishable from it by high pressure liquid chromatography [4].

References