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H-PHE-LEU-OH, also known as L-phenylalanine L-leucine dipeptide, is a dipeptide formed by the formal condensation of the carboxy group of L-phenylalanine with the amino group of L-leucine. It is a white to off-white powder and has potential applications in various industries.

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  • 3303-55-7 Structure
  • Basic information

    1. Product Name: H-PHE-LEU-OH
    2. Synonyms: PHE-LEU;H-PHE-LEU-OH;L-PHENYLALANYL-L-LEUCINE;L-PHE-LEU;L-Leucine, L-phenylalanyl-;phenylalanylleucine;L-Phe-L-Leu-OH;Phe-Leu-OH
    3. CAS NO:3303-55-7
    4. Molecular Formula: C15H22N2O3
    5. Molecular Weight: 278.35
    6. EINECS: N/A
    7. Product Categories: Amino Acid Derivatives
    8. Mol File: 3303-55-7.mol
  • Chemical Properties

    1. Melting Point: 258-260 °C
    2. Boiling Point: 516.2 °C at 760 mmHg
    3. Flash Point: 266 °C
    4. Appearance: White to off white powder
    5. Density: 1.144 g/cm3
    6. Vapor Pressure: 1.77E-11mmHg at 25°C
    7. Refractive Index: 1.544
    8. Storage Temp.: -15°C
    9. Solubility: N/A
    10. PKA: 3.15±0.10(Predicted)
    11. CAS DataBase Reference: H-PHE-LEU-OH(CAS DataBase Reference)
    12. NIST Chemistry Reference: H-PHE-LEU-OH(3303-55-7)
    13. EPA Substance Registry System: H-PHE-LEU-OH(3303-55-7)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 3303-55-7(Hazardous Substances Data)

3303-55-7 Usage

Uses

Used in Pharmaceutical Industry:
H-PHE-LEU-OH is used as a pharmaceutical candidate for the development of drugs targeting various diseases. Its unique structure and properties make it a promising molecule for drug discovery and design.
Used in Cosmetic Industry:
H-PHE-LEU-OH is used as an active ingredient in cosmetic products for its potential skin benefits. It may help improve skin elasticity, hydration, and overall skin health.
Used in Food Industry:
H-PHE-LEU-OH is used as a flavor enhancer and taste modifier in the food industry. Its unique taste profile can be utilized to improve the flavor and texture of various food products.
Used in Research:
H-PHE-LEU-OH is used as a research tool in the study of peptide synthesis, protein structure, and function. It can help researchers gain insights into the mechanisms of peptide-protein interactions and their implications in various biological processes.

Check Digit Verification of cas no

The CAS Registry Mumber 3303-55-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,3,0 and 3 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 3303-55:
(6*3)+(5*3)+(4*0)+(3*3)+(2*5)+(1*5)=57
57 % 10 = 7
So 3303-55-7 is a valid CAS Registry Number.
InChI:InChI=1/C15H22N2O3/c1-10(2)8-13(15(19)20)17-14(18)12(16)9-11-6-4-3-5-7-11/h3-7,10,12-13H,8-9,16H2,1-2H3,(H,17,18)(H,19,20)

3303-55-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name H-PHE-LEU-OH

1.2 Other means of identification

Product number -
Other names Phe-Leu-OH

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:3303-55-7 SDS

3303-55-7Relevant articles and documents

Multifunctional ionic liquid-bound polystyrene resin with high loading capacity as support in solid-phase peptide synthesis

Patra, Tanmoy,Karmakar, Sandip,Upadhyayula, Sreedevi

, p. 1531 - 1534 (2017)

Polystyrene resin-bound ionic liquids (PSILs) with high loading capacities were prepared by immobilizing multifunctional ionic liquids (ILs) on modified polystyrene (PS) resin and used in the solid phase peptide synthesis. Introduction of hydrophobic anio

γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis

Al Musaimi, Othman,El-Faham, Ayman,Basso, Alessandra,de la Torre, Beatriz G.,Albericio, Fernando

, (2019/08/26)

Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.

Layer-assembled 3D Bi2WO6 hierarchical architectures by Ti-doping for enhanced visible-light driven photocatalytic and photoelectrochemical performance

Arif, Muhammad,Zhang, Min,Yao, Jiacheng,Yin, Hongfei,Li, Pengfei,Hussain, Ijaz,Liu, Xiaoheng

, p. 878 - 893 (2019/04/17)

Layer-assembled three-dimensional (3D) catalysis gain substantial attention and widespread application in the field of photocatalysis and solar energy conversion. The 3D hierarchical architecture possesses large surface area and plenty reactive sites which contribute highly in catalysis performance. In this work we report a tetrabutyl titanate (TBT) assisted simultaneous approach of layer-assembled single-unit-cell 3D Bi2WO6 hierarchical architecture by Ti-doping. The Ti-doping beside its morphological effect can also generate crystal defects in the crystal lattice of Bi2WO6, resulting in highly enhanced visible-light driven photocatalytic performance towards highly stable refractory pollutants and profound photoelectrochemical ability. Moreover, the crystal defects mediated by Ti-doping can generate abundant oxygen vacancies which remarkably improve the selective adsorption towards different charges pollutants. Furthermore, the Ti-doping beside its great influence on the electron dynamic and band structure can also introduce the redox couples (Ti3+/Ti4+), resulting in significance enhancement in reactive oxygen species during photocatalytic reaction. The present work provides a valid route for constructing simultaneous approach of layer-assembled 3D hierarchical architecture and Ti-substitution in the crystal structure of Bi2WO6 with great improvement in photocatalytic and photoelectrochemical performance.

Microbial enantioselective removal of the N-benzyloxycarbonyl amino protecting group

Maurs, Michele,Acher, Francine,Azerad, Robert

, p. 22 - 26 (2012/10/29)

In order to deprotect N-carbobenzoxy-l-aminoacids (Cbz-AA) and related compounds, a series of microorganisms was selected from soil by enrichment cultures with Cbz-l-Glu as sole nitrogen source. A lyophilized whole-cell preparation of two Arthrobacter sp. strains grown on Cbz-Glu or Cbz-Gly exhibited a high cleavage activity. The conditions of hydrolysis have been optimized and a quantitative enantioselective deprotection of several Cbz-dl-amino acids was obtained, as well as the deprotection of N-carbamoylester derivatives of several synthetic amino compounds. The preparation of Cbz-d-allylglycine and l-allylglycine in high yield and high optical purity is described as an application of this method.

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi

, p. 2327 - 2335 (2011/05/02)

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.

Engineered transaminopeptidase, aminolysin-S for catalysis of peptide bond formation to give linear and cyclic dipeptides by one-pot reaction

Usuki, Hirokazu,Uesugi, Yoshiko,Arima, Jiro,Yamamoto, Yukihiro,Iwabuchi, Masaki,Hatanaka, Tadashi

supporting information; experimental part, p. 580 - 582 (2010/05/01)

Aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 was engineered into transaminopeptidase and used to catalyze an aminolysis reaction to give linear and cyclic dipeptides from cost-effective substrates such as the ester derivatives of amino

DPP4 INHIBITOR AND PHARMACEUTICAL APPLICATION THEREOF

-

Page/Page column 8-9, (2008/06/13)

The present invention provides a Dpp4 inhibitor which comprises a leucine derivative of the following formula (1) or a methionine derivative of the following formula (2): wherein each R1 and R3 represents a hydrogen atom (H) and an L-amino acid residue; R2 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline, alanine and phenylalanine) residue or L-amino-acid amide (except for proline amide, alanine amide and phenylalanine amide) residue; and R4 represents a hydroxyl group (OH), alkoxy group having 1 to 6 carbon atoms, amino group (NH2), alkylamino group having 1 to 6 carbon atoms, glycine residue, β-alanine residue, L-amino acid (except for proline and alanine) residue or L-amino-acid amide (except for proline amide and alanine amide) residue. These derivatives also act as autophagy regulators.

The molecular basis for the selection of captopril cis and trans conformations by angiotensin I converting enzyme

Tzakos, Andreas G.,Naqvi, Nawazish,Comporozos, Konstantinos,Pierattelli, Roberta,Theodorou, Vassiliki,Husain, Ahsan,Gerothanassis, Ioannis P.

, p. 5084 - 5087 (2007/10/03)

Enzyme-inhibitor recognition is considered one of the most fundamental aspects in the area of drug discovery. However, the molecular mechanism of this recognition process (induced fit or prebinding and adaptive selection among multiple conformers) in several cases remains unexplored. In order to shed light toward this step of the recognition process in the case of human angiotensin I converting enzyme (hACE) and its inhibitor captopril, we have established a novel combinatorial approach exploiting solution NMR, flexible docking calculations, mutagenesis, and enzymatic studies. We provide evidence that an equimolar ratio of the cis and trans states of captopril exists in solution and that the enzyme selects only the trans state of the inhibitor that presents architectural and stereoelectronic complementarity with its substrate binding groove.

Convenient solid-phase synthesis of oligopeptides using pentacoordinated phosphoranes with amino acid residue as building blocks

Li, Zhaolong,Fu, Hua,Gong, Hegui,Zhao, Yufen

, p. 170 - 177 (2007/10/03)

The reactive intermediates of pentacoordinated phosphoranes with amino acids (P(5)-AA) as building blocks, which were obtained by the reaction of O-phenylene phosphorochloridate with N,O-bis(trimethylsilyl)amino acids, were linked to a solid-phase support containing a hydroxymethyl polystyrene functional group. The first amino acid residue was coupled to the solid-phase support after washing the resin with organic solvent. Repeating the procedure led to oligopeptides linked on the resin. A series of free oligopeptides including tetra-Gly, di-Val, tri-Val, di-Leu, di-Phe, and Phe-Leu were obtained after cleavage from solid-phase support. The structure of these oligopeptides were determined by IR, 1H NMR, FAB-MS, and HPLC.

Enantioselective Enzymatic Cleavage of N-Benzyloxycarbonyl Groups

Patel, Ramesh N.,Nanduri, Venkata,Brzozowski, David,McNamee, Clyde,Banerjee, Amit

, p. 830 - 834 (2007/10/03)

A new enzymatic process for the enantioselective cleavage of N-benzyloxycarbonyl (Cbz) groups from protected amino acids and related compounds has been developed. The Cbz-deprotecting enzyme was isolated from cell extracts of Sphingomonas paucimobilis SC 16113 and purified to homogeneity. The purified protein has a molecular weight of 155,000 daltons and a subunit size of 44,000 daltons.

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