5c and d – oxidation rates at −80 °C were not tested). Finally, a non-cysteine containing peptide could be synthesized if no other method is acceptable. We have not observed any oxidation of peptide while it is stored in a freeze-dried state at −20 °C. We have characterized size profiles of cysteine-containing collagen peptides after either chemical cross-linking (CRPcys-XL), where such cross-linking allows formation CHIR 99021 of soluble

aggregates (Stokes Radius 8.6 nm) capable of activating platelets, or after air-induced cysteine oxidation upon storage. The latter gives rise to smaller polymers (1–6 triple helices) resulting from inter- and intra-helix oxidation of cysteine to disulphide bonds. This air-induced oxidation can be slowed by careful storage and handling.

We have also shown that cysteine facilitates strong adhesion of small collagen peptides to plastic and to glass, a valuable aid for surface-dependent analyses such as solid-phase adhesion assays. (a) Methods for gel filtration analysis are in Suppl. Sections 2.9–2.13. (b) Aggregation of platelets by CRPcys-XL is shown in Fig. S1. (c) Peptide oxidation states are shown in Figs. S2–S5 and Tables S1 and S2. Results are described in Suppl. Sections 3.8–3.11 and discussed in Sections 4.4 and 4.5. This work was supported by the British Heart Foundation (PG/08/011/24416). “
“The renin–angiotensin system (RAS) consists ABT-263 order of a number of peptide ligands and receptors whose distributions vary between species and, within species between individuals, according to the developmental stage, integrity and functional status of their different tissues. Such complexity reflects the many physiological and physiopathological functions carried out by the RAS which,

in addition, require a network of intertwined enzymatic pathways to produce the different angiotensin (Ang) peptides that act as effector molecules of the system. At first the RAS was thought as a typical endocrine system in which the effector hormone Ang II would be formed by a two-step reaction, whereby the Ang I initially released from angiotensinogen by circulating renin would then be converted into Ang II by the action of the however metalloprotease angiotensin converting enzyme (ACE). Despite the central role of this angiotensinogen–renin-ACE-Ang II axis for many of the functions carried out by the RAS, it became clear over the years that in some tissues Ang II could also be formed from Ang I by ACE-independent [5] or from Ang-(1-12) by renin-independent [20] pathways. The serine protease chymase, for instance, is the major enzyme that converts Ang I to Ang II in the human heart [32], while in the rat heart infused with Ang-(1-12) this enzyme appears to be responsible for most of the hemodynamic effects caused by the released Ang II [26].