Changes of Glutamine-peptides on Heating in Aqueous Media

Fukawa, Hideaki

doi:10.1246/nikkashi1948.88.4_459

Cited by 4 publications

(4 citation statements)

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“…Some experiments on the deamidation at 100°C of dipeptides and tripeptides that contain glutaminyl residues have been reported. 12 In these experiments the complicating effect of the end residues is evident. We have also begun some experiments on similar models that contain glutaminyl residues, and we also are studying the rates of deamidation of the glutaminyl and asparaginyl residue portions of cytochrome c, subtilisin, lysozyme, A-1 EAE brain protein, and histone IV.…”

mentioning

confidence: 84%

Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer

Robinson

McKerrow

Cary

1970

Proc. Natl. Acad. Sci. U.S.A.

228

118

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Abstract. Experiments on model peptides show that the rate of deamidation of asparaginyl residues depends strongly on the nature of neighboring residues. The natural distribution of glutaminyl and asparaginyl residues is ordered with respect to the biological lifetime of the peptides and the functional groups of the residues neighboring to glutaminyl and asparaginyl residues. The rates of deamidation of such amide peptides under physiological conditions could serve as useful timers of development and aging.The instability of the amino acids glutamine and asparagine with respect to hydrolytic deamidation of their functional side chains under relatively mild chemical conditions is well known. [1][2][3][4] The instability of glutaminyl and asparaginyl residues is a hazard during purification and primary structure determinations of peptides and proteins. In addition, now that Merrifield's solidphase peptide synthesis5-726 procedure has made the synthesis of peptides easily available to all laboratories, it seems likely that the differential stabilities of amide side chains during synthetic procedures will provide an additional problem.The experiments of T. Flatmark8-10'27 on the properties of the deamidated forms of horse heart cytochrome c show that variations occur in the rate of deamidation of different amides in the same protein molecule and that the deamidated cytochromes exhibit altered biological activity and structure. Deamidation has also been observed in numerous other proteins.11Why are these potentially unstable residues so widely distributed in nature? We suggest that controlled deamidation of glutaminyl and asparaginyl residues is a mechanism by which molecular and organismic development and aging are controlled.The rates of deamidation of glutaminyl and asparaginyl residues in proteins are probably determined by the primary and tertiary structures that govern distribution of amino acid residues surrounding the glutaminyl and asparaginyl residues in proteins. We have undertaken a study of the primary sequence dependence of deamidation of glutaminyl and asparaginyl residues in l)eptides.By comparing our results with the rates of deamidation of peptides of natural sequences and their corresponding proteins, we should also be able to make estimates of the tertiary structure dependence of deamidation. The results of our MAierrifield syntheses of the needed model peptides should aid in the prediction of difficulties during peptide synthesis and purification.

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mentioning

confidence: 84%

Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer

Robinson

McKerrow

Cary

1970

Proc. Natl. Acad. Sci. U.S.A.

228

118

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“…Masses calculated using Masslynx V 3.4.2 Modification is consistent with methionine sulfoxide at position 388 based upon fragmentation pattern in the mass spectrometer 3. Modification is consistent with isoAsp 270 based on mass analysis, NH 2 -terminal sequencing and Asp-N selectivity 4. Hydroxyproline 318 based on mass analysis, NH 2 -terminal sequencing and amino acid analysis 5.…”

mentioning

confidence: 73%

“…3 The % oxidation was determined from the peptide map, and is expressed as overall oxidation of the D335-L374 and D387-R396 peptides. 4 Bone Score, on a scale of 0-5.…”

Section: Correlation Of In-vitro and In-vivo Bioassays-mentioning

confidence: 99%

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Biomolecules in Tissue Engineered Medical Products (TEMPs): A Case Study of Recombinant Human Bone Morphogenetic Protein-2 (rhBMP-2)

Porter¹,

Rathore²,

Rouse³

et al. 2004

Journal of ASTM International

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rhBMP-2 is an osteoinductive protein that, when administered locally, results in the induction of new bone tissue at the site of implantation. The osteoinductive properties of rhBMP-2 first were demonstrated by implantation at ectopic (nonbony) sites in rodents. BMPs are the only protein factors known to induce new, ectopic bone. rhBMP-2/Absorbable Collagen Sponge (ACS) is a TEMP that combines rhBMP-2 with a matrix for implantation. rhBMP-2/ACS is used in long bone fracture repair and spinal fusion. The development of rhBMP-2 protein as the active ingredient in the rhBMP-2/ACS product is summarized. Four aspects of rhBMP-2 development are covered: protein structural characterization, functional characterization, purity analysis and design of comparability studies to support changes in the manufacturing process. Topics discussed include rhBMP-2 as a "biologic" and as a constituent of a combination TEMP. The lessons learned during the development of rhBMP-2/ACS may allow general insight into the development of future standards for TEMPs that contain biologically active proteins.

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Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures

McKerrow¹,

Robinson²

1971

Analytical Biochemistry

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Changes of Glutamine-peptides on Heating in Aqueous Media

Cited by 4 publications

References 0 publications

Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer

Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer

Biomolecules in Tissue Engineered Medical Products (TEMPs): A Case Study of Recombinant Human Bone Morphogenetic Protein-2 (rhBMP-2)

Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures

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