Far U.V. Spectra of Peptides

Ham, Joe S.; Platt, John R.

doi:10.1063/1.1700403

Cited by 88 publications

(16 citation statements)

References 8 publications

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“…The curves of the spectra resemble those reported in [54]. The peak observed at around 185 nm is attributed into an almost additive absorption by the carboxylic acid functional group (-COOH) [55]. Comparing the structures of the ribose and the carboxylic acid group (Table 1, The 2′-OH groups induce a regular and well-defined hydration pattern in the minor groove of the RNA helix.…”

Section: Hydroxyl Groups Are a Cause Of The Far-uv Absorbance Peaksupporting

confidence: 60%

“…The sugar-phosphate backbone where ribose (deoxyribose) holds the DNA together, allows it to dissolve in water, and is used by cells for specific functions. The far-UV-absorption spectra of two types of peptides (diglycine and triglycine) were measured in [55]. The curves of the spectra resemble those reported in [54].…”

Section: Hydroxyl Groups Are a Cause Of The Far-uv Absorbance Peakmentioning

confidence: 71%

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Water-SARS-CoV-2 Interaction-Based Mechanism Inhibiting Virus Attachment to Host Cells

Shalatonin

2020

Preprint

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Many studies showed that the enveloped viruses, including coronaviruses, HIV-1, and influenza inactivate significantly faster in water than the non-enveloped viruses. It looks that there is a certain mechanism controlling this phenomenon. However, the epidemic spread of SARS-CoV-2 indicates that this virus – water interaction mechanism is not effective enough to fully inhibit coronavirus reproduction. We hypothesized that a spatially extended layer of the ordered water molecules, formed around CoV due to the spike’s glycans – surrounding water interaction acts as a buffer inhibiting CoV motion and its attachment to the host cell receptor. There is experimental evidence that water molecules while interacting with glucans experience the long-range ordering and repulsive forces. Our findings revealed new features that can promote its interaction. It was shown that the glycans and water molecules have the same far ultraviolet (UV) absorbance peak at ~185 nm. This peak is a manifestation of the still little-known physical properties possessed by hydroxyl (OH) groups, including those contained in glycans and water molecules. Many studies show that the carbohydrate hydroxyl groups are a key element in the long-range antifreeze glycoproteins activity which is closely correlated with our issue. To further increase ice inhibition, a sugar-based (usually trehalose) water solution, further slowing down the water dynamics is commonly used. Our experiments with sugar-based compounds dissolved in water showed that in such solutions the UV absorbance at ~185 nm (activity of the OH groups) can be essentially increased with respect to the bulk water. The spike’s glycans – water long-range interaction, activated due to the dissolved sugar-based compound, creates the glass-like stabilizing hydration layer (like in case of the trehalose) effectively inhibiting the virus – host cell binding. It was shown that the chemical structures of the known compounds with proven inhibition of SARS-CoV-2 entry into host cells agree with our findings. The described approach can be effective against human immunodeficiency viruses, influenza viruses, and possibly other enveloped viruses. <br>

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Section: Hydroxyl Groups Are a Cause Of The Far-uv Absorbance Peaksupporting

confidence: 60%

Section: Hydroxyl Groups Are a Cause Of The Far-uv Absorbance Peakmentioning

confidence: 71%

Water-SARS-CoV-2 Interaction-Based Mechanism Inhibiting Virus Attachment to Host Cells

Shalatonin

2020

Preprint

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“… 1 – 3 The peptide bond in proteins has a strong absorption around 190 nm ( ε ∼ 7000 M –1 cm –1 ) and a weak absorption between 210 and 220 nm ( ε ∼ 100 M –1 cm –1 ). 4 – 7 Further, chromophores present in prosthetic groups and metal–ligand centres localized at enzyme active sites absorb in the visible (beyond 400 nm). 2 Accordingly, proteins devoid of aromatic amino acids, disulphide bonds, and active-site chromophores are expected to remain optically silent at wavelengths beyond 250 nm.…”

Section: Introductionmentioning

confidence: 99%

Near UV-Visible electronic absorption originating from charged amino acids in a monomeric protein

et al. 2017

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“…The lowest transition energy shows only very small variations as the number of peptide units increases. This result corresponds to the lack of an observable displacement of the longest wave length of absorption in proteins with respect to that of monopeptides [67]. The energy gap for the singlet-singlet transition is of the order of 5 eV, a result which seems to forbid the possibility of an intrinsic semiconductivity in proteins.…”

Section: Amentioning

confidence: 96%

Role of quantum chemical calculations in molecular biophysics with a historical perspective

Kukushkin

Jalkanen

2009

Theor Chem Acc

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We discuss how the basic principles of quantum chemistry and quantum mechanics can be and have been applied to a variety of problems in molecular biophysics. First, the historical development of quantum concepts in biophysics is discussed. Next, we describe a series of interesting applications of quantum chemical methods for studying biologically active molecules, molecular structures and some of the important processes which play a role in living organisms. We discuss the application of quantum chemistry to such processes as energy storage and transformation, and the transmission of genetic information. Quantum chemical approaches are essential to comprehend and understand the molecular nature of these processes. To conclude our work, we present a short discussion of the perspectives of quantum chemical methods in modern biophysics, the field of experimental and theoretical chiral vibrational and electronic spectroscopy.

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Far U.V. Spectra of Peptides

Abstract: The spectra of diglycyl, triglycyl, and glycine anhydride have been extended to 1800A in water solution. The peak observed near 1850A is attributed to an almost additive absorption by the —CONH— groups. The oscillator strength f is 0.27±0.07 per peptide group.

Cited by 88 publications

References 8 publications

Water-SARS-CoV-2 Interaction-Based Mechanism Inhibiting Virus Attachment to Host Cells

Water-SARS-CoV-2 Interaction-Based Mechanism Inhibiting Virus Attachment to Host Cells

Near UV-Visible electronic absorption originating from charged amino acids in a monomeric protein

Role of quantum chemical calculations in molecular biophysics with a historical perspective

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