N-Acetyl-Ser-Asp-Lys-Pro (TFA) is an endogenous tetrapeptide that is naturally produced in the bone marrow. It serves as a specific substrate for the N-terminal site of ACE, the enzyme responsible for angiotensin converting activity.
Arg-Gly-Asp-Ser is an integrin-binding sequence that inhibits integrin receptor function. It decreases systemic inflammation via inhibition of collagen-triggered activation of leukocytes and attenuates expression of inflammatory cytokines, MMP-9, and iNOS
PGlu-3-methyl-His-Pro-NH2 TFA enhances binding to pituitary TRH receptors, thereby increasing the stimulation of thyroid-stimulating hormone (TSH) release from the pituitary.
N-Formyl-Met-Ala-Ser is a peptide that binds to formyl peptide receptors on neutrophils. This N-Formylmethionine-containing peptide, known as fMet-Ala-Ser, is among the most potent and well-known peptides that interact with these receptors.
Arg-Gly-Asp-Cys TFAserves as the binding motif through which fibronectin interacts with cell adhesion molecules. This compound has the ability to hinder platelet aggregation and fibrinogen binding.