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Molecules
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New Insight of Bio-Mimetic Emulations
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New Insight of Bio-Mimetic Emulations

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".

Deadline for manuscript submissions: closed (30 March 2021) | Viewed by 6780

Special Issue Editor

Prof. Dr. Diego Ettore Liberati

E-Mail Website
Guest Editor
Department of Electronics, Information and Bioengineering, Politecnico, Piazza Leonardo da Vinci 32, 20133 Milan, Italy
Interests: systems and control; telecommunications; bioengineering

Special Issue Information

Dear Colleagues,

In the discussion among natural and synthetic drugs, a third path does naturally arise: to synthesize by mimicking nature. It may not always be the best approach, but evolution could probably have had reasons for many choices that have survived in nature, and this is worth to at least be taken into account. Such bio-mimetic emulation does encompass almost the entire spectrum from fully natural to in silico designs without any natural prior, thus allowing a multiplicity of approaches that will be welcome within our Special Issue. In particular, conjugation of statistical inference from data and mathematical deduction from known priors does seem useful to the task, without excluding any other mimicking approach.

Dr. Diego Ettore Liberati
Guest Editor

Manuscript Submission Information

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Keywords

  • bio-mimetic molecules
  • in silico design
  • inference from data observation
  • deduction from chemo-physical laws

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Published Papers (2 papers)

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Research

10 pages, 1366 KiB  
Article
Cyanovirin-N Binds Viral Envelope Proteins at the Low-Affinity Carbohydrate Binding Site without Direct Virus Neutralization Ability
by Irene Maier, Robert H. Schiestl and Georg Kontaxis
Molecules 2021, 26(12), 3621; https://doi.org/10.3390/molecules26123621 - 13 Jun 2021
Cited by 11 | Viewed by 2631
Abstract
Glycan-targeting antibodies and pseudo-antibodies have been extensively studied for their stoichiometry, avidity, and their interactions with the rapidly modifying glycan shield of influenza A. Broadly neutralizing antiviral agents bind in the same order when they neutralize enveloped viruses regardless of the location of [...] Read more.
Glycan-targeting antibodies and pseudo-antibodies have been extensively studied for their stoichiometry, avidity, and their interactions with the rapidly modifying glycan shield of influenza A. Broadly neutralizing antiviral agents bind in the same order when they neutralize enveloped viruses regardless of the location of epitopes to the host receptor binding site. Herein, we investigated the binding of cyanovirin-N (CV–N) to surface-expressed glycoproteins such as those of human immunodeficiency virus (HIV) gp120, hemagglutinin (HA), and Ebola (GP)1,2 and compared their binding affinities with the binding response to the trimer-folded gp140 using surface plasmon resonance (SPR). Binding-site knockout variants of an engineered dimeric CV–N molecule (CVN2) revealed a binding affinity that correlated with the number of (high-) affinity binding sites. Binding curves were specific for the interaction with N-linked glycans upon binding with two low-affinity carbohydrate binding sites. This biologically active assembly of a domain-swapped CVN2, or monomeric CV–N, bound to HA with a maximum KD of 2.7 nM. All three envelope spike proteins were recognized at a nanomolar KD, whereas binding to HIV neutralizing 2G12 by targeting HA and Ebola GP1,2 was measured in the µM range and specific for the bivalent binding scheme in SPR. In conclusion, invariant structural protein patterns provide a substrate for affinity maturation in the membrane-anchored HA regions, as well as the glycan shield on the membrane-distal HA top part. They can also induce high-affinity binding in antiviral CV–N to HA at two sites, and CVN2 binding is achieved at low-affinity binding sites. Full article
(This article belongs to the Special Issue New Insight of Bio-Mimetic Emulations)
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25 pages, 3512 KiB  
Article
Model-Based Optimization of a Fed-Batch Bioreactor for mAb Production Using a Hybridoma Cell Culture
by Gheorghe Maria
Molecules 2020, 25(23), 5648; https://doi.org/10.3390/molecules25235648 - 30 Nov 2020
Cited by 12 | Viewed by 3524
Abstract
Production of monoclonal antibodies (mAbs) is a well-known method used to synthesize a large number of identical antibodies, which are molecules of huge importance in medicine. Due to such reasons, intense efforts have been invested to maximize the mAbs production in [...] Read more.
Production of monoclonal antibodies (mAbs) is a well-known method used to synthesize a large number of identical antibodies, which are molecules of huge importance in medicine. Due to such reasons, intense efforts have been invested to maximize the mAbs production in bioreactors with hybridoma cell cultures. However, the optimal control of such sensitive bioreactors is an engineering problem difficult to solve due to the large number of state-variables with highly nonlinear dynamics, which often translates into a non-convex optimization problem that involves a significant number of decision (control) variables. Based on an adequate kinetic model adopted from the literature, this paper focuses on developing an in-silico (model-based, offline) numerical analysis of a fed-batch bioreactor (FBR) with an immobilized hybridoma culture to determine its optimal feeding policy by considering a small number of control variables, thus ensuring maximization of mAbs production. The obtained time stepwise optimal feeding policies of FBR were proven to obtain better performances than those of simple batch operation (BR) for all the verified alternatives in terms of raw material consumption and mAbs productivity. Several elements of novelty (i–iv) are pointed out in the “conclusions” section (e.g., considering the continuously added biomass as a control variable during FBR). Full article
(This article belongs to the Special Issue New Insight of Bio-Mimetic Emulations)
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