MBX2546 is an Influenza A Virus Fusion Inhibitor. MBX2546 binds to HA and inhibits HA-mediated membrane fusion. Both binding and stabilization of HA by MBX2546 are required for the inhibition of viral infection. Mutations in MBX2546-resistant influenza A
Tripeptidyl peptidase II (TPPII) is a serine peptidase of the subtilisin-type which removes tripeptides from the free NH2 terminus of oligopeptides. AAF-CMK is an irreversible inhibitor of TPPII commonly used at 10-100 μM. It does not significantly interfere with the chymotrypsin-like activity of the proteasome. AAF-CMK also inhibits bleomycin hydrolase and puromycin-sensitive aminopeptidase when used at 50 μM.
Antileukinate is a synthetic hexapeptide with an acetylated amino terminus and an amidated carboxyl terminus that inhibits the binding of CXC chemokines to the chemokine receptor CXCR2. It inhibits IL-8 binding to neutrophils (Ki = 2.7-13 μM), prevents neutrophil chemotaxis and β-glucuronidase release, and blocks IL-8-induced skin edema in rabbits. At 53 mg/kg, antileukinate has been shown to protect mice against acute pancreatitis and associated lung injury.
The ω-3 polyunsaturated fatty acids (PUFAs) found in fish oils provide cardiovascular benefits. Docosahexaenoic acid (DHA), a C22:6 PUFA, is the most abundant ω-3 fatty acid in neural tissues, especially in the retina and brain. It can be synthesized from other dietary ω-3 PUFAs or taken as a nutritional supplement. Docosahexaenoyl glycine consists of DHA with glycine attached at its carboxy terminus.
Squarunkin A hydrochloride 是一种有效的选择性UNC119-货物相互作用抑制剂。Squarunkin A hydrochloride 选择性地抑制Src 激酶 N 末端的肉豆蔻酰化肽与 UNC119A 的结合,IC50 值为 10 nm。Squarunkin A hydrochloride 会干扰细胞中Src 激酶的活化。
Transdermal Peptide is a 11-amino acid peptide, binds to Na+ K+-ATPase beta-subunit (ATP1B1), and enhances the transdermal delivery of many macromolecules. Transdermal Peptide (TD1) binds to ATP1B1, and mainly interacts with the C-terminus of ATP1B1 in yeast and mammalian cells. The interaction affects the expression and localization of ATP1B1 and epidermal structure, but can be antagonized by the exogenous competitor ATP1B1 or be inhibited by ouabain. Inhibition of Transdermal Peptide binding to ATP1B1 causes decreased delivery of macromolecular drugs across the skin[1]. [1]. Wang C, et al. Role of the Na(+) K(+)-ATPase beta-subunit in peptide-mediated transdermal drug delivery. Mol Pharm. 2015 Apr 6;12(4):1259-67.