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G2752

Sigma-Aldrich

Gly-Phe

≥97.0% (TLC)

Synonym(s):

Glycyl-L-phenylalanine

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About This Item

Linear Formula:
NH2CH2CONHCH(COOH)CH2C6H5
CAS Number:
3321-03-7
Molecular Weight:
222.24
Beilstein:
2279318
EC Number:
222-027-9
MDL number:
MFCD00065110
UNSPSC Code:
12352209
PubChem Substance ID:
24895100
NACRES:
NA.26

product name

Gly-Phe,

Assay

≥97.0% (TLC)

form

crystalline

color

white

mp

264 °C

storage temp.

−20°C

SMILES string

NCC(=O)N[C@@H](Cc1ccccc1)C(O)=O

InChI

1S/C11H14N2O3/c12-7-10(14)13-9(11(15)16)6-8-4-2-1-3-5-8/h1-5,9H,6-7,12H2,(H,13,14)(H,15,16)/t9-/m0/s1

InChI key

JBCLFWXMTIKCCB-VIFPVBQESA-N

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Related Categories

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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T Takarada et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 6(21), 3906-3913 (2000-12-29)
Oligopeptides are efficiently hydrolyzed by Ce(IV) to the corresponding amino acids under mild conditions. The pseudo first-order rate constants for the hydrolysis of H-Gly-Phe-OH and H-Gly-Gly-OH at pH 7.0 and 50 degrees C are 3.5 x 10(-1) and 2.8 x
Susan Weng Larsen et al.
European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 22(5), 399-408 (2004-07-22)
Oil-based depot formulations may constitute a future delivery method for small peptides. Thus, a requirement is attainment of sufficient oil solubility for such active compounds. A model dipeptide (Gly-Phe) has been converted into lipophilic prodrugs by esterification at the C-terminal
Kuniyo Inouye et al.
Bioscience, biotechnology, and biochemistry, 71(8), 2083-2086 (2007-08-11)
The aim of this study was to improve the performance of affinity gels containing glycyl-D-phenylalanine (Gly-D-Phe) as a ligand to thermolysin. Gly-D-Phe was immobilized to the resin through spacers of varying chain lengths. The resulting affinity gels had spacer chain
Roderick Y H Lim et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(25), 9512-9517 (2006-06-14)
Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding
S J Reshkin et al.
The American journal of physiology, 260(3 Pt 2), R563-R569 (1991-03-01)
The transport mechanisms for the dipeptide glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanine (Phe) were characterized in fish intestinal brush-border membrane vesicles (BBMV). Gly-Phe was rapidly hydrolyzed only intravesicularly with almost total hydrolysis occurring even at 10 s. Dipeptide uptake was not stimulated
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