cck (27 33) (non sulfated)

CCK (27-33) is a C-terminal fragment of CCK , a peptide hormone found in the intestine and brain that stimulates digestion, mediates satiety, and is involved in anxiety. Non-sulfated CCK (27-33) inhibits binding of [3H]naloxone in rat cerebellum membranes (IC50 = 4 uM) and inhibits electrically-stimulated contraction of isolated guinea pig ileum (IC50 = 17 uM), an effect that can be reversed by naloxone. Unlike sulfated CCK (27-33), the non-sulfated form does not reduce exploratory behavior in mice when administered at doses up to 1 uMol/kg.

CCK Octapeptide, non-sulfated acetate is a synthetic desulfated peptide of cholecystokinin.

CCK (26-31) is an N-terminal fragment of CCK , a peptide hormone found in the intestine and brain that stimulates digestion, mediates satiety, and is involved in anxiety. The sulfated form of CCK (26-31) inhibits binding of [125I]CCK-33 to guinea pig cortical membranes by 21% when used at a concentration of 0.1 mM.

CCK (26-31) is an N-terminal fragment of CCK , a peptide hormone found in the intestine and brain that stimulates digestion, mediates satiety, and is involved in anxiety.

CCK (26-30) is an N-terminal fragment of CCK , a peptide hormone found in the intestine and brain that stimulates digestion, mediates satiety, and is involved in anxiety. The sulfated form of CCK (26-30) inhibits binding of [125I]CCK-33 to guinea pig cortical membranes by 10% when used at a concentration of 0.1 mM.

[Thr28, Nle31]-Cholecystokinin (25-33) is a bioactive peptide analog of Cholecystokinin (CCK) that functions as both a hormone and neurotransmitter in the gastrointestinal and central nervous systems, playing a role in satiation by inhibiting food intake. Compared to native CCK8, this analog displays enhanced stability in acidic environments and resistance to air oxidation, due to the substitution of Methionine with Threonine at position 28 and Norleucine at position 31. Structurally, it features a gamma-turn at Thr4, followed by a Gly5-separated helical region encompassing the C-terminal residues.