Gly-Ala-OH (BAT-005001)
* For research use only

Catalog number
CAS number
Molecular Formula
Molecular Weight
Glycyl-L-alanine; H-Gly-Ala-OH; (S)-2-(2-Aminoacetamido)Propanoic Acid
White powder
≥ 99% (TLC, Assay by titration)
Melting Point
230°C (dec.)
Boiling Point
417.4ºC at 760 mmHg
Store at 2-8 °C
InChI Key
Canonical SMILES
1.Glycyl-L-alanine: a multi-temperature neutron study.
Capelli SC1, Bürgi HB2, Mason SA3, Jayatilaka D4. Acta Crystallogr C Struct Chem. 2014 Oct;70(Pt 10):949-52. doi: 10.1107/S2053229614019809. Epub 2014 Sep 28.
Neutron diffraction data have been collected at 12, 50, 150 and 295 K for the dipeptide glycyl-L-alanine, C5H10N2O3, in order to obtain accurate positional and anisotropic displacement parameters for the H atoms. The values of these parameters serve as a benchmark for assessing the equivalent parameters obtained from a so-called Hirshfeld-atom refinement of X-ray diffraction data described elsewhere [Capelli et al. (2014). IUCrJ, 1, 361-379]. The flexibility of the glycyl-L-alanine molecule in the solid and the hydrogen-bonding interactions as a function of temperature are also considered.
2.Solvation and hydrogen bonding in alanine- and glycine-containing dipeptides probed using solution- and solid-state NMR spectroscopy.
Bhate MP1, Woodard JC, Mehta MA. J Am Chem Soc. 2009 Jul 15;131(27):9579-89. doi: 10.1021/ja902917s.
The NMR chemical shift is a sensitive reporter of peptide secondary structure and its solvation environment, and it is potentially rich with information about both backbone dihedral angles and hydrogen bonding. We report results from solution- and solid-state (13)C and (15)N NMR studies of four zwitterionic model dipeptides, L-alanyl-L-alanine, L-alanyl-glycine, glycyl-L-alanine, and glycyl-glycine, in which we attempt to isolate structural and environmental contributions to the chemical shift. We have mapped hydrogen-bonding patterns in the crystalline states of these dipeptides using the published crystal structures and correlated them with (13)C and (15)N magic angle spinning chemical shift data. To aid in the interpretation of the solvated chemical shifts, we performed ab initio quantum chemical calculations to determine the low-energy conformers and their chemical shifts. Assuming low energy barriers to interconversion between thermally accessible conformers, we compare the Boltzmann-averaged chemical shifts with the experimentally determined solvated-state shifts.
3.Preparation of platinum(IV) complexes with dipeptide and diimine. X-ray crystal structure and 195Pt NMR spectra.
Watabe M1, Fukuda H, Kitsukawa K, Nakajima H, Yukawa Y, Igarashi S, Fujii Y, Takayama T. J Inorg Biochem. 2006 Oct;100(10):1653-9. Epub 2006 Jun 9.
We prepared platinum(IV) complexes containing dipeptide and diimine or diamine, the [PtCl(dipeptide-N,N,O)(diimine or diamine)]Cl complex, where -N,N,O means dipeptide coordinated as a tridentate chelate, dipeptide=glycylglycine (NH(2)CH(2)CON(-)CH(2)COO(-), digly, where two protons of dipeptide are detached when the dipeptide coordinates to metal ion as a tridentate chelate), glycyl-L-alanine (NH(2)CH(2)CON(-)CHCH(3)COO(-), gly-L-ala), L-alanylglycine (NH(2)CH CH(3)CON(-)CH(2)COO(-), L-alagly), or L-alanyl-L-alanine (NH(2)CHCH(3)CON(-)CHCH(3)COO(-), dil-ala), and diimine or diamine=bipyridine (bpy), ethylenediamine (en), N-methylethylenediamine (N-Me-en), or N,N'-dimethylethylenediamine (N,N'-diMe-en). In the complexes containing gly-L-ala or dil-ala, two separate peaks of the (195)Pt NMR spectra of the [PtCl(dipeptide-N,N,O)(diimine or diamine)]Cl complexes appeared in, but in the complexes containing digly or L-alagly, one peak which contained two overlapped signals appeared.
4.Water structure around dipeptides in aqueous solutions.
McLain SE1, Soper AK, Watts A. Eur Biophys J. 2008 Jun;37(5):647-55. doi: 10.1007/s00249-008-0292-1. Epub 2008 Mar 11.
The bulk water structure around small peptide fragments--glycyl-L-alanine, glycyl-L-proline and L:-alanyl-L-proline-has been determined by a combination of neutron diffraction with isotopic substitution and empirical potential structural refinement techniques. The addition of each of the dipeptides to water gives rise to decreased water-water coordination in the surrounding water solvent. Additionally, both the Ow-Ow radial distribution functions and the water-water spatial density functions in all of the solutions indicate an electrostrictive effect in the second water coordination shell of the bulk water network. This effect is not observed in similar experiments on the amino acid L: -proline alone in solution, which is one component of two of the peptides measured here.
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Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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