The fields of biological and medical physics and biomedical engineering are broad, multidisciplinary and dynamic. They lie at the crossroads of frontier research in physics, biology, chemistry, and medicine. The Biological and Medical Physics, Biomedical Engineering Series is intended to be comprehensive, covering a broad range of topics important to the study of the physical, chemical and biological sciences. Its goal is to provide scientists and engineers with textbooks, monographs, and reference works to address the growing need for information.

Biological and medical physics, biomedical engineering

In situ and real-time characterization of protein secondary structures at interfaces is important in biological and bioengineering sciences, yet remains technically challenging. In this study, we used chiral sum frequency generation (SFG) spectroscopy to establish a set of vibrational optical markers for characterizing protein secondary structures at interfaces. We discovered that the N–H stretches along the peptide backbones of α-helices can be detected in chiral SFG spectra. We further observed that the chiral vibrational signatures of the N–H stretch together with the peptide amide I are unique to α-helix, β-sheet, and random coil at interfaces. Using these chiral vibrational signatures, we studied the aggregation of human islet amyloid polypeptide (hIAPP), which is implicated in type II diabetes. We observed in situ and in real time the misfolding of hIAPP from random coils to α-helices and then β-sheets upon interaction with a lipid–water interface. Our findings show that chiral SFG spectroscopy is a...

Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces

Model calculations are performed on the amide-I infrared (IR) bands of globular proteins. Coupling between peptide groups is introduced by the transition dipole coupling (TDC) mechanism. Good agreement is obtained between the calculated and observed amide-I band envelopes. In order to obtain detailed information on the structure-spectrum correlation, 3-D doorway-state theory is worked out and is applied to the spectra thus calculated. The E 1 - mode like motions of (alpha) -helices are shown to have large contributions to the IR intensity in the 1640 - 1630 cm -1 region of myoglobin, settling the question as to the origin of such bands observed for highly helical proteins. The differences in the amide-I band envelopes between (alpha) -lactalbumin and lysozyme are most probably due to the structural differences between the (alpha) -helical parts near the N-termini of these proteins.

Model calculations on the amide-I infrared bands of globular proteins

http://users.rowan.edu/~wuc/gallery/PaperPDB/029_COSB.pdf

Coarse-grained models for protein aggregation.

Amyloid formation has been implicated in the pathology of over 20 human diseases, but the rational design of amyloid inhibitors is hampered by a lack of structural information about amyloid-inhibitor complexes. We use isotope labelling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin (the peptide responsible for islet amyloid formation in type 2 diabetes) with a known inhibitor (rat amylin). Based on its sequence, rat amylin should block formation of the C-terminal β-sheet, but at 8 h after mixing, rat amylin blocks the N-terminal β-sheet instead. At 24 h after mixing, rat amylin blocks neither β-sheet and forms its own β-sheet, most probably on the outside of the human fibrils. This is striking, because rat amylin is natively disordered and not previously known to form amyloid β-sheets. The results show that even seemingly intuitive inhibitors may function by unforeseen and complex structural processes.

/pdf/two-dimensional-infrared-spectroscopy-reveals-the-complex-54ejfu11xz.pdf

Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor

Solution structures of rat amylin peptide: simulation, theory, and experiment

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Solution structures of rat amylin peptide: simulation, theory, and experiment