Aspartyl-serine
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| Category | Others |
| Catalog number | BBF-05502 |
| CAS | 6403-13-0 |
| Molecular Weight | 220.18 |
| Molecular Formula | C7H12N2O6 |
| Purity | ≥95% |
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Description
Aspartyl-serine is a dipeptide composed of aspartic acid and serine. It is an incomplete breakdown product of protein digestion or protein catabolism.
Specification
| Synonyms | L-Serine, L-a-aspartyl-; Aspartylserine; (S)-3-Amino-N-((S)-1-carboxy-2-hydroxy-ethyl)-succinamic acid; Asp-Ser; α-L-Asparagyl-L-serine; L-Asp-L-Ser; H-DS-OH; L-alpha-aspartyl-L-serine; (S)-3-amino-4-(((S)-1-carboxy-2-hydroxyethyl)amino)-4-oxobutanoic acid |
| Sequence | H-Asp-Ser-OH |
| IUPAC Name | (3S)-3-amino-4-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid |
| Canonical SMILES | C(C(C(=O)NC(CO)C(=O)O)N)C(=O)O |
| InChI | InChI=1S/C7H12N2O6/c8-3(1-5(11)12)6(13)9-4(2-10)7(14)15/h3-4,10H,1-2,8H2,(H,9,13)(H,11,12)(H,14,15)/t3-,4-/m0/s1 |
| InChI Key | DWBZEJHQQIURML-IMJSIDKUSA-N |
Properties
| Appearance | Solid |
| Boiling Point | 629.8±55.0°C at 760 mmHg |
| Density | 1.6±0.1 g/cm3 |
| Solubility | Soluble in Water |
Reference Reading
1. Arginine-glycine-aspartic acid functional branched semi-interpenetrating hydrogels
Richard A Plenderleith, Christopher J Pateman, Cornelia Rodenburg, John W Haycock, Frederik Claeyssens, Chris Sammon, Stephen Rimmer Soft Matter. 2015 Oct 14;11(38):7567-7578. doi: 10.1039/c5sm00695c.
For the first time a series of functional hydrogels based on semi-interpenetrating networks with both branched and crosslinked polymer components have been prepared and we show the successful use of these materials as substrates for cell culture. The materials consist of highly branched poly(N-isopropyl acrylamide)s with peptide functionalised end groups in a continuous phase of crosslinked poly(vinyl pyrrolidone). Functionalisation of the end groups of the branched polymer component with the GRGDS peptide produces a hydrogel that supports cell adhesion and proliferation. The materials provide a new synthetic functional biomaterial that has many of the features of extracellular matrix, and as such can be used to support tissue regeneration and cell culture. This class of high water content hydrogel material has important advantages over other functional hydrogels in its synthesis and does not require post-processing modifications nor are functional-monomers, which change the polymerisation process, required. Thus, the systems are amenable to large scale and bespoke manufacturing using conventional moulding or additive manufacturing techniques. Processing using additive manufacturing is exemplified by producing tubes using microstereolithography.
2. Proteolysis and antigen presentation by MHC class II molecules
Paula Wolf Bryant, Ana-Maria Lennon-Duménil, Edda Fiebiger, Cécile Lagaudrière-Gesbert, Hidde L Ploegh Adv Immunol. 2002;80:71-114. doi: 10.1016/s0065-2776(02)80013-x.
Proteolysis is the primary mechanism used by all cells not only to dispose of unwanted proteins but also to regulate protein function and maintain cellular homeostasis. Proteases that reside in the endocytic pathway are the principal actors of terminal protein degradation. The proteases contained in the endocytic pathway are classified into four major groups based on the active-site amino acid used by the enzyme to hydrolyze amide bonds of proteins: cysteine, aspartyl, serine, and metalloproteases. The presentation of peptide antigens by major histocompatibility complex (MHC) class II molecules is strictly dependent on the action of proteases. Class II molecules scour the endocytic pathway for antigenic peptides to bind and present at the cell surface for recognition by CD4+ T cells. The specialized cell types that support antigen presentation by class II molecules are commonly referred to as professional antigen presenting cells (APCs), which include bone marrow-derived B lymphocytes, dendritic cells (DCs), and macrophages. In addition, the expression of certain endocytic proteases is regulated either at the level of gene transcription or enzyme maturation and their activity is controlled by the presence of endogenous protease inhibitors.
3. Mechanisms by which extracellular matrix components induce osteoblast apoptosis
C S Adams, I M Shapiro Connect Tissue Res. 2003;44 Suppl 1:230-9.
Bone cell apoptosis is seen at sites of active turnover. We hypothesize that at these sites, factors released from resorbing bone induce apoptosis of vicinal cells. Related to this observation, earlier studies indicate that an elevation in the level of inorganic phosphate ions combined with a modest increase in the calcium (Ca2+) concentration, or a rise in the local concentration of RGD-containing peptides promote osteoblast apoptosis. The aim of the current investigation is to elucidate the mechanism by which these extracellular matrix components induce bone cell apoptosis. The data presented in this study clearly demonstrate that osteoblasts are sensitive to peptide fragments and solubilized mineral ions. It is reasonable to expect that these apoptogens would be generated by osteoclasts during resorption of the extracellular bone matrix. We suggest that these components conspire to regulate bone cell function. In terms of the mechanism by which these agents activate apoptosis, it is clear that while they share common pathways, there are some differences in the mechanism of apoptosis. These differences appear to be upstream of caspase activation. The observation that two such pathways exist lends strength to the notion that apoptosis is carefully regulated in bone and that signals from both matrix components act together to trigger the remodeling process.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
