The primary structure of collagen, the major protein in connective tissue of mammals, comprises of repeating triads [(_LPro‐_LHyp‐Gly)_n, P1, _LHyp being 4R‐hydroxy‐lProline)] in a single strand that adopts left‐handed polyproline II type helix. Three such single stranded helices wind around each another and held together by interchain H‐bonds to form right‐handed triple helix. This manuscript reports on collagen derived from its mirror image triad [(_DPro‐_DHyp‐Gly)_n, P2, _DHyp being 4S‐hydroxy‐_DProline) and its 4‐amino analogue (_DPro‐_DAmp‐Gly)_n P4, _DAmp being 4S‐amino‐_DProline that form corresponding spiegelmeric triplexes. The amino L‐collagen peptide (_LPro‐_LAmp‐Gly)_n P3 and its D‐analogue P4 show higher thermal stabilities compared to 4‐hydroxy‐lProline collagen peptides P1 and P2. The enantiomeric peptide pairs show mirror image CD profiles and identical thermal stability, with ionizable 4‐amino group in P3 and P4 imparting pH dependent triplex stability. Upon cold mixing of the L‐ and D‐collagen peptides, different morphological nanostructures arise from inter triplex peptide association. When the peptides are hot mixed (annealed), the inter peptide association occurs via interaction of single stranded peptide chains of opposite handedness leading to networked gel formation in P1 and P2, while the charged peptides P3 and P4 show more ordered nanofibers, different from the enantiomerically pure peptides. The nanocomposites of such chiral hybrid peptides may have not only interesting physicomorphology, but also biological properties that need exploration.

中文翻译：

---

镜像异构的4R / S-羟基/氨基-L / D-脯氨酰胶原肽：自组装结构的构象和形态

胶原蛋白的主要结构是哺乳动物结缔组织中的主要蛋白质，由单链重复的三联体[（_L Pro‐ _L Hyp‐Gly）_n，P1，_L Hyp为4 R‐羟基l脯氨酸）组成，采用左旋脯氨酸II型螺旋。三个这样的单链螺旋彼此缠绕，并通过链间氢键结合在一起，形成右旋三螺旋。对胶原这个手稿报告从与其镜像三联[（衍生_d亲_d羟脯氨酸-甘氨酸）_ñ，P2，_d羟脯氨酸为4小号羟基_d脯氨酸）和它的4-氨基类似物（_d亲_d安培-甘氨酸）_ñ P4，_d安培为4小号氨基_d脯氨酸该形式对应spiegelmeric三链。氨基L-胶原肽（_L Pro- _L Amp-Gly）_n P3及其D-类似物P4与4-羟基l脯氨酸胶原蛋白肽P1和P2相比具有更高的热稳定性。对映体肽对显示镜像CD轮廓和相同的热稳定性，在P3和P4中具有可电离的4-氨基赋予pH依赖的三链体稳定性。L-和D-胶原蛋白肽冷混合后，三联体间肽缔合会产生不同的形态纳米结构。当将肽段热混合（退火）时，肽段间的缔合通过相反手性的单链肽链相互作用而发生，从而在P1和P2中形成网络化的凝胶形成，而带电的肽段P3和P4显示出更有序的纳米纤维，不同于对映体纯的肽。这种手性杂合肽的纳米复合物不仅具有令人感兴趣的物理形态学，而且还具有需要探索的生物学特性。