484-42-4

Usage

Uses

Used in Pharmaceutical Industry:
Angiotensin I, Human is used as a precursor for the production of angiotensin II, which is a potent vasoconstrictor involved in blood pressure regulation and fluid balance. It is essential for the development of drugs targeting the RAS, which can be used to treat hypertension and other cardiovascular conditions.
Used in Research and Development:
Angiotensin I, Human serves as an important research tool for studying the RAS and its role in various physiological processes. It is used in the development of new drugs and therapies targeting the RAS, as well as in the investigation of the underlying mechanisms of hypertension, heart failure, and other related conditions.
Used in Diagnostic Applications:
Angiotensin I, Human can be used as a diagnostic marker to assess the activity of the RAS in patients with cardiovascular diseases. Measuring the levels of angiotensin I and its conversion to angiotensin II can provide valuable information about the functionality of the RAS and help in the diagnosis and monitoring of various cardiovascular conditions.
Used in Drug Delivery Systems:
Angiotensin I, Human can be employed in the development of targeted drug delivery systems, particularly for the delivery of antihypertensive and cardiovascular drugs. By utilizing the RAS as a target, these systems can potentially improve the efficacy and specificity of drug treatments for hypertension and other related conditions.

InChI:InChI=1/C62H89N17O14/c1-7-35(6)51(78-56(87)44(25-37-17-19-40(80)20-18-37)74-58(89)50(34(4)5)77-53(84)42(15-11-21-68-62(64)65)71-52(83)41(63)28-49(81)82)59(90)75-46(27-39-30-67-32-70-39)60(91)79-22-12-16-48(79)57(88)73-43(24-36-13-9-8-10-14-36)54(85)72-45(26-38-29-66-31-69-38)55(86)76-47(61(92)93)23-33(2)3/h8-10,13-14,17-20,29-35,41-48,50-51,80H,7,11-12,15-16,21-28,63H2,1-6H3,(H,66,69)(H,67,70)(H,71,83)(H,72,85)(H,73,88)(H,74,89)(H,75,90)(H,76,86)(H,77,84)(H,78,87)(H,81,82)(H,92,93)(H4,64,65,68)/t35-,41-,42-,43-,44-,45-,46-,47-,48-,50-,51-/m0/s1

Upstream product

• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 13734-41-3 t-Boc-L-valine 
• 13139-16-7 N-(tert-butyloxycarbonyl)-L-isoleucine 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 13836-37-8 Boc-Arg(Tos)-OH 
• 73821-95-1 Boc-Asp(O-cyclohexyl)-OH 
• 47689-67-8 (S)-3-[4-(2-Bromo-benzyloxycarbonyloxy)-phenyl]-2-tert-butoxycarbonylamino-propionic acid 
• 35899-43-5 Boc-His(Tos)-OH 
• 68858-20-8 Fmoc-Val-OH 
• 71989-31-6 Fmoc-Pro-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-14-5 Fmoc-(tBu)Asp-OH 
• 71989-23-6 Fmoc-Ile-OH 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 

Downstream Products

• 72-18-4 L-valine 
• 56-84-8 L-Aspartic acid 
• 74-79-3 L-arginine 
• 61-90-5 L-leucine 
• 73-32-5 L-isoleucine 
• 63-91-2 L-phenylalanine 
• 60-18-4 L-tyrosine 
• 147-85-3 L-proline 
• 71-00-1 L-histidine 
• 4474-91-3 angiotensin II 
• 7763-65-7 (S)-2-[(S)-2-Amino-3-(1H-imidazol-4-yl)-propionylamino]-4-methyl-pentanoic acid 
• 42014-19-7 IHPFHL 
• 52580-29-7 Asp-Arg-Val-Tyr 
• 146958-86-3 C₆₉H₉₄N₁₈O₁₄S 

Relevant academic research and scientific papers

HPLC FREE PURIFICATION OF PEPTIDES BY THE USE OF NEW CAPPING AND CAPTURE REAGENTS

The present disclosure relates to the use of a capping and capture reagent in solid phase peptide synthesis. The present disclosure further relates to a method of solid phase peptide synthesis, wherein a capping and capture reagent according to the present disclosure is used. The present disclosure further relates to a method for purification of a (full-length) synthetic peptide via use of a capping and capture reagent according to the present disclosure. The present disclosure also relates to a kit comprising a capping and capture reagent according to the present disclosure and an amino oxy resin or a hydrazine resin and the use of the kit.

Boosting Fmoc Solid-Phase Peptide Synthesis by Ultrasonication

We investigated the ultrasonication-mediated effects on the Fmoc-based solid-phase peptide synthesis (SPPS). Our study culminated with the development of an ultrasound-assisted strategy (US-SPPS) that allowed for the synthesis of different biologically active peptides (up to 44-mer), with a remarkable savings of material and reaction time. Noteworthy, ultrasonic irradiation did not exacerbate the main side reactions and improved the synthesis of peptides endowed with "difficult sequences", placing the US-SPPS among the current high-efficient peptide synthetic strategies.

A Vinylogous Photocleavage Strategy Allows Direct Photocaging of Backbone Amide Structure

Side-chain modifications that respond to external stimuli provide a convenient approach to control macromolecular structure and function. Responsive modification of backbone amide structure represents a direct and powerful alternative to impact folding and function. Here, we describe a new photocaging method using histidine-directed backbone modification to selectively modify peptides and proteins at the amide N-H bond. A new vinylogous photocleavage method allows photorelease of the backbone modification and, with it, restoration of function.

Controlled formation of peptide bonds in the gas phase

Photoexcitation (using 157 nm vacuum ultraviolet radiation) of proton-bound peptide complexes leads to water elimination and the formation of longer amino acid chains. Thus, it appears that proton-bound dimers are long-lived intermediates along the pathway to peptide formation. Product specificity can be controlled by selection of specific complexes and the incorporation of blocking groups at the N- or C-termini. The product peptide sequences are confirmed using collision-induced dissociation.

Solid-phase peptide synthesis in highly loaded conditions

The use of very highly substituted resins has been avoided for peptide synthesis due to the aggravation of chain-chain interactions within beads. To better evaluate this problem, a combined solvation-peptide synthesis approach was herein developed taking as models, several peptide-resins and with peptide contents values increasing up to near 85%. Influence of peptide sequence and loading to solvation characteristics of these compounds was observed. Moreover, chain-chain distance and chain concentration within the bead were also calculated in different loaded conditions. Of note, a severe shrinking of beads occurred during the α-amine deprotonation step only when in heavily loaded resins, thus suggesting the need for the modification of the solvent system at this step. Finally, the yields of different syntheses in low and heavily loaded conditions were comparable, thus indicating the feasibility of applying this latter "prohibitive" chemical synthesis protocol. We thought these results might be basically credited to the possibility, without the need of increasing molar excess of reactants, of carrying out the coupling reaction in higher concentration of reactants - near three to seven folds - favored by the use of smaller amount of resin. Additionally, the alteration in the solvent system at the α-amine deprotonation step might be also improving the peptide synthesis when in heavily loaded experimental protocol.

GnRH antagonists being modified in positions 5 and 6

Peptides are provided which have improved duration of GnRH antagonistic properties. These antagonists may be used to regulate fertility and to treat steroid-dependent tumors and for other short-term and long-term treatment indications. These antagonists have a derivative of aminoPhe or its equivalent in the 5- or the 5- and 6-positions. This derivative is modified so as to contain a carbamoyl group or heterocycle, including a urea moiety, in its side chain. Decapeptides having the formula: Ac-D-2Nal-D-4Cpa-D-3Pal-Ser-4Aph(L-hydroorotyl)-D-4Amf(Q2)-Leu-Lys(isopropyl)-Pro-Xaa10, wherein Q2is Cbm or MeCbm and Xaa10is D-Ala-ol or Ala-ol are particularly effective and continue to exhibit very substantial suppression of LH secretion at 96 hours following injection.

Solid support matrices with memories and combinatorial libraries therefrom

Combinations, called matrices with memories, of matrix materials that are encoded with an optically readable code are provided. The matrix materials are those that are used in as supports in solid phase chemical and biochemical syntheses, immunoassays and hybridization reactions. The matrix materials may additionally include fluophors or other luminescent moieties to produce luminescing matrices with memories. The memories include electronic and optical storage media and also include optical memories, such as bar codes and other machine-readable codes. By virtue of this combination, molecules and biological particles, such as phage and viral particles and cells, that are in proximity or in physical contact with the matrix combination can be labeled by programming the memory with identifying information and can be identified by retrieving the stored information. Combinations of matrix materials, memories, and linked molecules and biological materials are also provided. The combinations have a multiplicity of applications, including combinatorial chemistry, isolation and purification of target macromolecules, capture and detection of macromolecules for analytical purposes, selective removal of contaminants, enzymatic catalysis, cell sorting, drug delivery, chemical modification and other uses. Methods for tagging molecules, biological particles and matrix support materials, immunoassays, receptor binding assays, scintillation proximity assays, non-radioactive proximity assays, and other methods are also provided.

Remotely programmable matrices with memories and uses thereof

Combinations, called matrices with memories, of matrix materials with remotely addressable or remotely programmable recording devices that contain at least one data storage unit are provided. The matrix materials are those that are used in as supports in solid phase chemical and biochemical syntheses, immunoassays and hybridization reactions. The matrix materials may additionally include fluophors or other luminescent moieties to produce luminescing matrices with memories. The data storage units are non-volatile antifuse memories or volatile memories, such as EEPROMS, DRAMS or flash memory. By virtue of this combination, molecules and biological particles, such as phage and viral particles and cells, that are in proximity or in physical contact with the matrix combination can be labeled by programming the memory with identifying information and can be identified by retrieving the stored information. Combinations of matrix materials, memories, and linked molecules and biological materials are also provided. The combinations have a multiplicity of applications, including combinatorial chemistry, isolation and purification of target macromolecules, capture and detection of macromolecules for analytical purposes, selective removal of contaminants, enzymatic catalysis, cell sorting, drug delivery, chemical modification and other uses. Methods for electronically tagging molecules, biological particles and matrix support materials, immunoassays, receptor binding assays, scintillation proximity assays, non-radioactive proximity assays, and other methods are also provided.

Psycho-pharmacological peptides

Disclosed are novel (6-17) β-endorphin fragments which possess a derivatized lysine at site 9. The peptides have the amino acid sequence according to the general formula: wherein X is a derivatized lysine, selected from the group Lys-Ac, Lys(Z), des-Lys, A2hy, Nle, Met, Leu or Lys [(ar)alkyl]; R1 is Ser, Ala or Pro; R2 is L-Gln, D-Gln, Glu(tyramine) or iodine-containing derivatives thereof; and R3 is L-Leu, Leu-NHCH3, Met, Phe, Phe(Cl), Phe(I), Cha, Mag, Val, (HO)Leu, Bua or Bug. Methods of making the fragments are also described.