Vasonatrin Peptide (VNP) Trifluoroacetate

Vasonatrin Peptide (VNP) Trifluoroacetate contains a structured sequence balancing polar, charged, and hydrophobic residues that shape receptor-binding characteristics. The trifluoroacetate counterion improves solubility and handling. Researchers explore its folding behavior and dynamic transitions in aqueous media. Applications include signaling-motif analysis, structural modeling, and peptide engineering.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Vasonatrin Peptide (VNP) Trifluoroacetate(CAS 141676-35-9)

CAT No: R2656

CAS No:141676-35-9

Synonyms/Alias:Vasonatrin Peptide (VNP) Trifluoroacetate;141676-35-9;FV108689;Vasonatrin Peptide (VNP) trifluoroacetate salt;H-Gly-Leu-Ser-Lys-Gly-Cys-Phe-Gly-Leu-Lys-Leu-Asp-Arg-Ile-Gly-Ser-Met-Ser-Gly-Leu-Gly -Cys-Asn-Ser-Phe-Arg-Tyr-OH; H-GLSKGCFGLKLDRIG SMSGLGCNSFRY-OH;

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M.F/Formula
C126H199F3N36O38S3
M.W/Mr.
2979.3
Sequence
One Letter Code:GLSKGCFGLKLDRIGSMSGLGCNSFRY
Three Letter Code:H-Gly-Leu-Ser-Lys-Gly-Cys(1)-Phe-Gly-Leu-Lys-Leu-Asp-DL-Arg-Ile-Gly-Ser-Met-Ser-Gly-Leu-Gly-Cys(1)-Asn-Ser-Phe-Arg-Tyr-OH.TFA

Vasonatrin Peptide (VNP) Trifluoroacetate is a synthetic peptide composed of sequences derived from both atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP), resulting in a unique chimeric molecule. Designed for advanced research applications, VNP Trifluoroacetate exhibits distinct biochemical properties, combining the vasodilatory and natriuretic effects attributed to its parent peptides. Its structure enables it to interact with natriuretic peptide receptors, influencing various physiological pathways related to vascular tone, fluid balance, and cellular signaling. The trifluoroacetate form ensures stability and solubility, making it suitable for diverse experimental settings in molecular biology, pharmacology, and physiological research. Researchers value this compound for its ability to elucidate the mechanisms underlying natriuretic peptide signaling and its potential to model complex cardiovascular and renal processes in vitro and in vivo.

Cardiovascular Research: Vasonatrin Peptide serves as a valuable tool for investigating the regulation of vascular tone and blood pressure. Its hybrid structure allows researchers to study the combined effects of ANP and CNP pathways, particularly in the context of vasodilation and endothelial function. By applying VNP in isolated vessel assays or perfused organ systems, scientists can assess its impact on vascular smooth muscle relaxation, nitric oxide production, and cyclic GMP signaling. These studies contribute to a deeper understanding of how natriuretic peptides modulate cardiovascular homeostasis and provide insight into the cross-talk between different peptide receptors in vascular tissues.

Renal Physiology Studies: In renal research, VNP Trifluoroacetate is instrumental for exploring mechanisms of natriuresis and diuresis. Its dual action enables precise dissection of sodium and water excretion pathways in kidney tissues or cell models. Researchers utilize this peptide to stimulate natriuretic peptide receptors in renal cells, monitoring changes in electrolyte transport, glomerular filtration rate, and tubular function. Such investigations shed light on the physiological roles of natriuretic peptides in maintaining fluid and electrolyte balance, as well as their interactions with other hormonal systems involved in renal regulation.

Signal Transduction Analysis: The use of Vasonatrin Peptide in signal transduction studies allows for the mapping of intracellular pathways activated by natriuretic peptide receptors. By employing this peptide in cultured cells or tissue preparations, scientists can monitor downstream signaling events, such as cyclic GMP production, protein kinase G activation, and modulation of ion channels. These analyses help clarify the molecular mechanisms by which natriuretic peptides exert their effects, facilitating the identification of novel targets for therapeutic intervention and advancing the broader field of receptor pharmacology.

Cellular Proliferation and Apoptosis: Researchers investigating cell growth and survival pathways leverage the properties of VNP Trifluoroacetate to study its influence on cellular proliferation and apoptosis. The peptide's ability to activate natriuretic peptide receptors provides a model for examining how these signaling cascades regulate cell cycle progression, differentiation, and programmed cell death. Experimental applications include the assessment of VNP's effects on cultured vascular smooth muscle cells, endothelial cells, or kidney epithelial cells, offering valuable insights into tissue remodeling and repair mechanisms.

Pharmacological Screening: Vasonatrin Peptide is frequently employed in pharmacological assays to evaluate the activity of novel compounds targeting natriuretic peptide receptors. By serving as a reference agonist or functional probe, it enables high-throughput screening of receptor modulators, antagonists, or allosteric regulators. These applications are critical for drug discovery and the development of new molecular entities aimed at modulating natriuretic peptide pathways for research purposes.

Vascular Endothelial Function: Further extending its research utility, VNP Trifluoroacetate is used to probe the mechanisms underlying endothelial cell function and barrier integrity. Studies often involve the peptide's application to cultured endothelial monolayers or ex vivo vessel preparations to assess its effects on permeability, inflammatory responses, and oxidative stress. These investigations contribute to a comprehensive understanding of how natriuretic peptides influence vascular health and the maintenance of endothelial homeostasis. With its multifaceted applications across cardiovascular, renal, cellular, and pharmacological research, Vasonatrin Peptide (VNP) Trifluoroacetate stands as a versatile and indispensable compound for scientists advancing the field of natriuretic peptide biology.

InChI
InChI=1S/C124H198N36O36S3.C2HF3O2/c1-12-68(10)101-121(194)139-57-97(170)143-88(59-162)116(189)150-77(37-42-197-11)108(181)157-87(58-161)105(178)138-54-95(168)141-78(43-64(2)3)103(176)136-56-99(172)145-92(120(193)154-84(50-93(128)166)114(187)159-90(61-164)118(191)153-83(48-70-27-17-14-18-28-70)113(186)148-75(31-23-40-133-123(129)130)107(180)156-86(122(195)196)49-71-33-35-72(165)36-34-71)63-199-198-62-91(144-98(171)55-135-102(175)73(29-19-21-38-125)146-117(190)89(60-163)158-111(184)79(44-65(4)5)140-94(167)52-127)119(192)152-82(47-69-25-15-13-16-26-69)104(177)137-53-96(169)142-80(45-66(6)7)110(183)147-74(30-20-22-39-126)106(179)151-81(46-67(8)9)112(185)155-85(51-100(173)174)115(188)149-76(109(182)160-101)32-24-41-134-124(131)132;3-2(4,5)1(6)7/h13-18,25-28,33-36,64-68,73-92,101,161-165H,12,19-24,29-32,37-63,125-127H2,1-11H3,(H2,128,166)(H,135,175)(H,136,176)(H,137,177)(H,138,178)(H,139,194)(H,140,167)(H,141,168)(H,142,169)(H,143,170)(H,144,171)(H,145,172)(H,146,190)(H,147,183)(H,148,186)(H,149,188)(H,150,189)(H,151,179)(H,152,192)(H,153,191)(H,154,193)(H,155,185)(H,156,180)(H,157,181)(H,158,184)(H,159,187)(H,160,182)(H,173,174)(H,195,196)(H4,129,130,133)(H4,131,132,134);(H,6,7)/t68-,73-,74-,75-,76?,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,101-;/m0./s1
InChI Key
IQSOKNKKIFXBDJ-MUQIQXKDSA-N

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