Biologically Active Proteins & Peptides

Neurotensin is a biologically active peptide that functions as a neuromodulator, influencing neurotransmission and neuroendocrine responses. It interacts specifically with neurotensin receptors, triggering intracellular signaling cascades that affect calcium mobilization and cyclic AMP levels. This peptide is involved in regulating appetite and pain perception, showcasing its role in diverse physiological processes. Its unique structure allows for specific receptor binding, facilitating distinct biological effects.

Angiotensin II [Sar1 Ile8] is a potent biologically active peptide that plays a crucial role in the renin-angiotensin system. It exhibits strong affinity for angiotensin receptors, leading to vasoconstriction and modulation of blood pressure. This peptide influences cellular signaling pathways, particularly those involving phospholipase C and protein kinase C, resulting in increased intracellular calcium levels. Its structural modifications enhance receptor selectivity and stability, impacting cardiovascular and renal functions.

Octreotide Acetate is a synthetic octapeptide that mimics somatostatin, exhibiting unique interactions with specific receptors in the endocrine system. Its binding affinity influences various signaling cascades, particularly inhibiting adenylate cyclase activity, which modulates cyclic AMP levels. This peptide's conformation allows for enhanced stability and prolonged action, affecting cellular processes such as hormone secretion and cell proliferation. Its distinct molecular interactions contribute to its regulatory roles in physiological functions.

Penetratin is a cell-penetrating peptide characterized by its ability to traverse cellular membranes through unique interactions with lipid bilayers. Its amphipathic nature facilitates the formation of transient pores, enhancing membrane permeability. This peptide engages in specific electrostatic and hydrophobic interactions, promoting efficient internalization into target cells. The kinetics of its cellular uptake are influenced by factors such as concentration and incubation time, allowing for versatile applications in molecular delivery systems.

Hel 13-5 is a biologically active compound known for its unique reactivity as an acid halide, which enables it to form covalent bonds with nucleophiles in biological systems. Its electrophilic nature allows for selective modification of amino acids in proteins, influencing enzymatic activity and protein interactions. The compound exhibits rapid reaction kinetics, making it a potent agent for altering cellular pathways and modulating biochemical processes through targeted acylation.

(Arg)9 is a biologically active peptide characterized by its high affinity for specific receptors, facilitating unique molecular interactions that influence cellular signaling pathways. Its structure promotes effective binding to target proteins, enhancing or inhibiting their functions. The compound's stability in physiological conditions allows for sustained activity, while its ability to penetrate cellular membranes enables it to engage in diverse biochemical processes, impacting gene expression and cellular responses.

Biotin - TAT (47 - 57) is a biologically active compound known for its role in modulating enzymatic activity through specific protein interactions. Its unique structure allows for selective binding to biotin-dependent enzymes, influencing metabolic pathways. The compound exhibits remarkable stability, enabling it to maintain functionality under various conditions. Additionally, its capacity to form complexes with co-factors enhances its reactivity, facilitating critical biochemical transformations within cellular environments.

L-Alanyl-L-proline is a biologically active dipeptide that plays a significant role in cellular signaling and protein synthesis. Its unique structure promotes specific interactions with receptors and enzymes, influencing various metabolic pathways. The compound exhibits a propensity for forming stable hydrogen bonds, enhancing its solubility and reactivity in aqueous environments. Additionally, its ability to act as a chiral building block contributes to the diversity of peptide synthesis, impacting protein folding and function.

Boc-Gly-Pro-OH is a biologically active compound characterized by its ability to engage in selective molecular interactions, particularly through its amine and carboxylic acid functional groups. This dipeptide exhibits unique conformational flexibility, allowing it to adopt various spatial arrangements that facilitate enzyme recognition. Its protective Boc group enhances stability and reactivity, making it a versatile intermediate in peptide synthesis. The compound's hydrophilic nature promotes solubility, influencing its behavior in biological systems.

Proteasome Inhibitor II is a biologically active compound known for its selective binding to proteasome subunits, disrupting protein degradation pathways. This inhibitor alters cellular homeostasis by stabilizing regulatory proteins, leading to significant changes in cellular signaling. Its unique structure allows for specific interactions with the proteasome's active site, influencing reaction kinetics and enhancing the accumulation of polyubiquitinated substrates. The compound's distinct physicochemical properties contribute to its efficacy in modulating proteolytic processes.