Chemistry:Allysine

From HandWiki
Allysine
Skeletal formula of zwitterion
Ball-and-stick model of the L-allysine molecule as a zwitteiron
Names
Preferred IUPAC name
(2S)-2-Amino-6-oxohexanoic acid
Other names
2-aminoadipate semialdehyde, 2-amino-5-formylvaleric acid, norvaline, 6-oxo-DL-norleucine
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
KEGG
MeSH allysine
UNII
Properties
C6H11NO3
Molar mass 145.158 g·mol−1
Density 1.74g/cm3
Boiling point 295.2 °C (563.4 °F; 568.3 K)
Hazards
Flash point 132.3 °C (270.1 °F; 405.4 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Allysine is a derivative of lysine, used in the production of elastin and collagen. It is produced by the actions of the enzyme lysyl oxidase in the extracellular matrix and is essential in the crosslink formation that stabilizes collagen and elastin.[1]

Clinical relevance

Large quantities of elastin and collagen present in tissue may lead to metastasis: spread of disease. Fibrous tissue containing oxidized collagen may result in a condition known as fibrosis. The oxidation of lysine residues present in collagen creates the aldehyde, aminoadipic-δ-semialdehyde (allysine). Increased allysine concentration in tissues has been correlated to the presence of fibrosis.[2] To qualify protein carbonyls in biological systems, most research studies use the dinitrophenylhydrazine (DNPH) process. The study of particular protein carbonyls, such as allysine, reveals more about specific redox processes and mechanisms at the molecular level. [3] Allysine and its oxidation product, α- amino adipic acid (α-AA), have been discovered to also be diabetes risk indicators. To get a better understanding of this concept, human serum albumin was incubated for 32 hours at 37 degrees Celsius in the presence of FeCl3 (25 μM) and increasing glucose concentrations. Both allysine and α-AA levels were found to rise as glucose levels increased which lead to the depletion of tryptophan. Regarding the underlying functions of tryptophan and its metabolites, depletion of tryptophan and its metabolites may result in additional physiological problems such as coronary artery disease and neurological complications.[4]

Allysine quantification

Allysine can be reacted with sodium 2-naphthol-6-sulfonate to produce a fluorescent bis-naphtol allysine product. Allysine can then be quantified through use of high-performance liquid chromatography (HPLC). This method of detection was used show allysine has a 2.5 higher concentration in fibrotic vs. normal tissue.[5]

See also

References

  1. "The cross-linking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to alpha-aminoadipic-delta-semialdehyde (allysine) by an extract from bone". Proceedings of the National Academy of Sciences of the United States of America 61 (2): 708–16. October 1968. doi:10.1073/pnas.61.2.708. PMID 5246001. Bibcode1968PNAS...61..708P. 
  2. "68Ga-NODAGA-Indole: An Allysine-Reactive Positron Emission Tomography Probe for Molecular Imaging of Pulmonary Fibrogenesis". Journal of the American Chemical Society 141 (14): 5593–5596. April 2019. doi:10.1021/jacs.8b12342. PMID 30908032. 
  3. "Formation of allysine in β-lactoglobulin and myofibrillar proteins by glyoxal and methylglyoxal: Impact on water-holding capacity and in vitro digestibility". Food Chemistry 271: 87–93. January 2019. doi:10.1016/j.foodchem.2018.07.167. PMID 30236745. 
  4. "Allysine and α-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage to Human Serum Albumin under Pathological Glucose Concentrations". Antioxidants 10 (3): 474. March 2021. doi:10.3390/antiox10030474. PMID 33802856. 
  5. "High sensitivity HPLC method for determination of the allysine concentration in tissue by use of a naphthol derivative". Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences 1064: 7–13. October 2017. doi:10.1016/j.jchromb.2017.08.032. PMID 28886479.