Rama Sashank Madhurapantula

Illinois Institute of Technology

Rama Sashank Madhurapantula is a research assistant professor in the Biology Department, Illinois Institute of Technology, Chicago. His current research involves developing microscopy techniques to establish macroscopic stress vs strain relations in body tissues that present mixed-tissue compositions, in conjunction with X-ray diffraction scanning techniques to establish tissue composition. His doctoral work was in understanding molecular changes to collagens with diseases and changes in fibrous structures such as myelin. In recognition of scientific endeavors and achievements, Dr. Madhurapantula was elected as chair to the Fiber Diffraction Special Interest Group of the American Crystallographic Association in 2020 and awarded the Margaret C. Etter Student Lecturer award in 2014.

1books edited

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Latest work with IntechOpen by Rama Sashank Madhurapantula

Understanding extracellular matrix (ECM) structure and function is important for developing biomedical applications that are as close to ‘native’ as possible. Written by pioneering scientists from all over the world, this book reports research and new developments in the field of collagen structure, function, and biomechanics and discusses the relevance of hyaluronic acid and its therapeutic uses. It gives readers a glimpse of what is current in this area and we hope it piques their interest in learning more about ECM biology.

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Extracellular Matrix

Edited by Rama Sashank Madhurapantula

Chapters authored

X-Ray Diffraction Detects D-Periodic Location of Native Collagen Crosslinks In Situ and Those Resulting from Non- Enzymatic Glycation

By Rama Sashank Madhurapantula and Joseph P.R.O. Orgel

Synchrotron based X-ray diffraction experiments can be highly effective in the study of mammalian connective tissues and related disease. It has been employed here to observe changes in the structure of Extra-Cellular Matrix (ECM), induced in an ex vivo tissue based model of the disease process underlying diabetes. Pathological changes to the structure and organization of the fibrillar collagens within the ECM, such as the formation of non-enzymatic crosslinks in diabetes and normal aging, have been shown to play an important role in the progression of such maladies. However, without direct, quantified and specific knowledge of where in the molecular packing these changes occur, development of therapeutic interventions has been impeded. In vivo, the result of non-enzymatic glycosylation i.e. glycation, is the formation of sugar-mediated crosslinks, aka advanced glycation end-products (AGEs), within the native D-periodic structure of type I collagen. The locations for the formation of these crosslinks have, until now, been inferred from indirect or comparatively low resolution data under conditions likely to induce experimental artifacts. We present here X-ray diffraction derived data, collected from whole hydrated and intact isomorphously derivatized tendons, that indicate the location of both native (existing) and AGE crosslinks in situ of D-periodic fibrillar collagen.

Part of the book: Accelerator Physics

Rama Sashank Madhurapantula

Latest work with IntechOpen by Rama Sashank Madhurapantula

Extracellular Matrix

Chapters authored

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