Boc-Gly-Gly-Phe-Gly-OH - CAS 187794-49-6

Boc-Gly-Gly-Phe-Gly-OH - CAS 187794-49-6 Catalog number: BADC-00622

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Boc-Gly-Gly-Phe-Gly-OH is a self-assembly of N- and C-protected tetrapeptide. It is also a protease-cleavable linker for antibody-drug conjugates (ADCs).

Category
ADCs Linker
Product Name
Boc-Gly-Gly-Phe-Gly-OH
CAS
187794-49-6
Catalog Number
BADC-00622
Molecular Formula
C20H28N4O7
Molecular Weight
436.46
Boc-Gly-Gly-Phe-Gly-OH

Ordering Information

Catalog Number Size Price Quantity
BADC-00622 250 mg $198
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Description
Boc-Gly-Gly-Phe-Gly-OH is a self-assembly of N- and C-protected tetrapeptide. It is also a protease-cleavable linker for antibody-drug conjugates (ADCs).
Synonyms
N-tert-butoxycarbonyl-glycyl-glycyl-L-phenylalanyl-glycine; N-(tert-butoxycarbonyl)-glycylglycyl-L-phenylalanylglycine; (S)-12-Benzyl-2,2-dimethyl-4,7,10,13-tetraoxo-3-oxa-5,8,11,14-tetraazahexadecan-16-oic acid
IUPAC Name
2-[[(2S)-2-[[2-[[2-[(2-methylpropan-2-yl)oxycarbonylamino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]acetic acid
Canonical SMILES
CC(C)(C)OC(=O)NCC(=O)NCC(=O)NC(CC1=CC=CC=C1)C(=O)NCC(=O)O
InChI
InChI=1S/C20H28N4O7/c1-20(2,3)31-19(30)23-10-15(25)21-11-16(26)24-14(18(29)22-12-17(27)28)9-13-7-5-4-6-8-13/h4-8,14H,9-12H2,1-3H3,(H,21,25)(H,22,29)(H,23,30)(H,24,26)(H,27,28)/t14-/m0/s1
InChIKey
PTUJJIPXBJJLLV-AWEZNQCLSA-N
Sequence
Boc-GGFG-OH
Density
1.263±0.06 g/cm3 (Predicted)
Solubility
Soluble in water
Appearance
Powder
Purity
>95%
Shipping
Room temperature
Storage
Store at -20°C
Boiling Point
838.6±65.0°C (Predicted)

Boc-Gly-Gly-Phe-Gly-OH, also known as N-(tert-Butoxycarbonyl)-glycyl-glycyl-L-phenylalanylglycine, is a peptide featuring notable versatility in research and pharmaceutical applications. First and foremost, it is extensively employed in the field of proteomics for protein structure and function analysis. The peptide serves as a valuable standard or control in mass spectrometry and chromatography, allowing researchers to better understand protein interactions and enzymatic activities critical to cellular processes. By offering insight into the conformational properties of proteins in different environments, Boc-Gly-Gly-Phe-Gly-OH significantly aids in elucidating the mechanisms underlying disease pathogenesis, especially in neurodegenerative and metabolic disorders.

Another significant application of Boc-Gly-Gly-Phe-Gly-OH is in the development of novel therapeutic agents. The peptide can be included in drug design and testing processes to evaluate pharmacokinetics, stability, and bioavailability of new compounds. Studying the interactions of this peptide with potential drug molecules enables scientists to identify and optimize lead compounds with better efficacy and reduced side effects. Moreover, the peptide’s structural properties make it an ideal candidate for mimicking certain endogenous peptides, thus paving the way for innovative treatments for diseases such as cancer, diabetes, and inflammatory disorders.

In the realm of synthetic biology, Boc-Gly-Gly-Phe-Gly-OH plays a crucial role in the design and synthesis of artificial proteins and peptides. As a building block, it is used to construct larger peptide chains that imitate natural biological functions, aiding in the creation of biomaterials with specific properties tailored for medical applications. For instance, these engineered peptides can be used in tissue engineering, wound healing, and the development of novel scaffolds for regenerative medicine. The ability to precisely control the peptide sequences enhances the understanding of protein engineering and can potentially lead to breakthrough innovations in biomedicine.

1. Reactivity of cosmetic UV filters towards skin proteins: model studies with Boc-lysine, Boc-Gly-Phe-Gly-Lys-OH, BSA and gelatin
C Stiefel, W Schwack Int J Cosmet Sci. 2014 Dec;36(6):561-70. doi: 10.1111/ics.12157. Epub 2014 Sep 11.
Objective: Organic UV filters are used as active ingredients in most sunscreens and also in a variety of daily care products. Their good (photo) stability is of special interest to guarantee protective function and to prevent interactions with the human skin. Due to the mostly electrophilic character of the UV filters, reactions with nucleophilic protein moieties like lysine side chains are conceivable. Prior studies showed that the UV filters octocrylene (OCR), butyl methoxydibenzoylmethane (BM-DBM), ethylhexyl salicylate (EHS), ethylhexyl methoxycinnamate (EHMC), benzophenone-3 (BP-3), ethylhexyl triazone (EHT) and dibenzoylmethane (DBM) were able to covalently bind to an HPTLC amino phase and the amino acid models ethanolamine and butylamine after slightly heating and/or radiation. Methods: Boc-protected lysine, the tetrapeptide Boc-Gly-Phe-Gly-Lys-OH, bovine serum albumin (BSA) and porcine gelatin were used as more complex models to determine the reactivity of the mentioned UV filters towards skin proteins under thermal or UV irradiation conditions. Results: After gentle heating at 37°C, benzophenone imines were identified as reaction products of BP-3 and OCR with Boc-lysine and the tetrapeptide, whereas DBM and BM-DBM yielded enamines. For EHMC, a Michael-type reaction occurred, which resulted in addition of Boc-lysine or the tetrapeptide to the conjugated double bond. Ester aminolysis of EHS and EHT mainly afforded the corresponding amides. Reactions of the UV filters with BSA changed the UV spectrum of BSA, generally associated with an increase of the absorption strength in the UVA or UVB range. For all protein models, the UV filters showed an increasing reactivity in the order EHT < EHMC < EHS < BP-3 < OCR < DBM < BM-DBM. Conclusion: Especially the UV absorbers BM-DBM, OCR and BP-3, which are seen as common allergens or photoallergens, showed a high reactivity towards the different skin protein models. As the formation of protein adducts is recognized as important key element in the induction of skin sensitization, the results of this study can contribute to a better understanding of the underlying chemical mechanisms of such reactions.
2. [Syntheses of oligopeptides related to the insulin sequence B 22-25 (Arg-Gly-Phe-Phe) (author's transl)]
K Eisele Hoppe Seylers Z Physiol Chem. 1975 Jun;356(6):845-54.
Syntheses of peptides with the sequences Gly-Phe, Gly-Phe-Phe, Arg-Gly-Phe and Arg-Gly-Phe-Phe are described. They were performed with the free acids, methyl esters and caramides. The peptides correspond partially or directly to the insulin sequence B 22 - 25 (Arg-Gly-Phe-Phe), the tetrapeptide amide or tetrapeptide methyl ester of which shows insulin-like activity (l.c.[1,2]). For testing the structural specificity of the arginyl residue, the following peptides were also synthesised: NG-NO2-Arg-Gly-Phe-Phe-NH2 and -OMe, Orn-Gly-Phe-Phe-NH2 and Cit-Gly-Phe-Phe--NH2. In connection with the above, the syntheses of the new derivatives Nalpha,Ndelta-Z2-L-ornithine p-nitrophenyl ester and N-Boc-L-citrulline p-nitrophenyl ester are described. All peptides were synthesised conventionally.
3. The effects of various peptides on the thermotropic properties of phosphatidylcholine bilayers
R M Epand, J M Sturtevant Biophys Chem. 1984 Jun;19(4):355-62. doi: 10.1016/0301-4622(84)87018-0.
The effects of an amino acid derivative (N-benzoyl-L-argininamide), four small peptides (Phe-Gly-Phe-Gly, gastrin-related peptide (Trp-Met-Arg-Phe-NH2), tetragastrin (Trp-Met-Asp-Phe-NH2), pentagastrin (Boc-beta Ala-Trp-Met-Asp-Phe-NH2] and one medium-sized peptide, glucagon (29 residues), on the gel-to-liquid crystalline transition of a multilamellar suspension of dimyristoylphosphatidylcholine have been studied by means of high-sensitivity differential scanning calorimetry. At low concentrations of added solutes, the temperature at which the excess apparent specific heat in the gel-to-liquid crystalline phase transition of the lipid is maximal is lowered by an amount proportional to the total concentration of the peptide, with proportionality constants ranging from -0.018 K mM-1 for Phe-Gly-Phe-Gly to -3.1 K mM-1 for the gastrin-related peptide. The lipid mixtures involving the first two solutes listed above exhibited approximately symmetrical curves of excess apparent specific heat vs. temperature. The curves for the other solutes were asymmetric, and could be well represented as the sum of either two or three two-state curves. The asymmetry, which was especially pronounced in the cases of pentagastrin and glucagon, thus appeared to be due to the presence of components having lower and/or higher transition temperatures than that of the lipid. Pentagastrin and glucagon (R.M. Epand and J.M. Sturtevant, Biochemistry 20 (1981) 4603) have much smaller effects on the gel-to-liquid crystalline phase transition of dipalmitoylphosphatidylcholine than on that of the dimyristoyl analog.
The molarity calculator equation

Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Historical Records: Boc-Gly-Gly-Phe-Gly-OH
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