Scientific Program

Conference Series Ltd invites all the participants across the globe to attend 20th Global Congress on Biotechnology Park Inn by Radisson Hotel London, UK.

Day 1 :

Keynote Forum

Peter J F Henderson

Astbury Centre for Structural Molecular Biology - University of Leeds, UK

Keynote: Kinetic and molecular dissection of coupled ion-substrate membrane transport proteins

Time : 09:30-10:10

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Peter J F Henderson photo

Peter J F Henderson is a Professor of Biochemistry and Molecular Biology in the University of Leeds. He obtained his BSc in 1965 and PhD in 1968, both in Biochemistry,
at the University of Bristol. After Postdoctoral training at the Enzyme Institute, Madison, University of Wisconsin and in the Department of Biochemistry at Leicester, he
became a University Lecturer in 1973. In 1975 he moved to the Department of Biochemistry at Cambridge, where he became Reader in Molecular Biology of Membranes in
1990. He has held Visiting Professorships in Japan, Canada and Australia. He was Scientifi c Director of the European Membrane Protein (EMeP) consortium 2003-2008,
Coordinator of the European Drug Initiative for Channels and Transporters (EDICT) 2008-2012 and held Leverhulme Trust Emeritus Research Fellowships in 2001-2002
and 2014-2017. He has published over 200 scientifi c papers in the fi elds of Membrane Transport, Enzyme Kinetics and Structural Biology.


The Mhp1 Na+, -hydantoin membrane symport protein from Microbacterium liquefaciens is a paradigm for the nucleobasecation-
symport, NCS-1, family of transport proteins found widely in archaebacteria, bacteria, yeasts and plants. Th eir
metabolic roles include the capture by cells of nitrogen compounds and vitamins from the environment. Mhp1 is also a
structural model for the huge range of ‘5-helix-inverted-repeat’ superfamily of proteins, because, unusually, crystal structures
are available for its open-outwards, occluded, and open-inward conformations. Here we accomplish a detailed dynamic model
of the partial reactions in an alternating access cycle of membrane transport derived from substrate binding studies to the
purifi ed Mhp1 protein by combining novel mass spectrometry, stopped-fl ow and steady state kinetic analyses and mutagenesis.
Th e mechanism of coupling substrate transport to the Na+, -gradient is revealed during a sequence of mostly reversible kinetic
steps that explain how transfer of substrate across the membrane is aff ected by changes in conformational states. Th e AceI
H+/substrate antiport protein from Acinetobacter baumannii is a paradigm for the proteobacterial antimicrobial compound
effl ux (PACE) family of drug effl ux proteins found dispersed throughout the Proteobacteria. AceI contributes to the resistance
of Acinetobacter baumannii towards the widely used antiseptic, chlorhexidine. Currently there is little structural information
about the PACE family of transport proteins, but progress towards understanding the recognition of substrates and cations by
AceI and its homologues will be discussed.

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Magali Remaud Simeon photo

Magali Remaud Simeon is Professor at the National Institute of Applied Sciences of Toulouse and is head of the Catalysis and Enzyme Molecular Engineering group of
the “Laboratoire d’Ingénierie des Système Biologiques and Procédé (LISBP). She received her PhD in Biochemistry from the University of Toulouse and was Post-Doc
at the University of Pennsylvania. She has co-authored more than 150 papers and is co-inventor of 22 patents. Her research activities focus on Enzyme Engineering
for white biotechnology, green chemistry, health, food/feed industries and synthetic biology. They cover enzyme structure/activity relationship studies, kinetic resolution,
evolution combining both rational and combinatorial approaches, and applications to the synthesis of glycans, glycoconjugates and various synthons of interest. Her work
is currently focused on the search and generation of enzymes displaying new specifi cities and improved catalytic properties. Her objective is to open new trajectories for
biomass transformation. To this end, she specifi cally targets the integration of tailored enzymes in chemo-enzymatic cascades, new metabolic pathways or enzyme-based


The exploration of the natural diversity, through data mining, functional genomics and/or metagenomics is an effi cient mean
to discover enzymes showing new functions or improved performances. Th ese approaches can be further completed or run
in parallel with semi-rational protein engineering based on structure/function studies or directed molecular evolution inspired
from nature. Which of these alternatives are the best ones, in terms of eff ort, rapidity and effi ciency? Th is is an open question
to which a defi nite answer can be hardly formulated a priori. For illustration, we will take a few examples from our most recent
work on glucansucrases from GH13 and GH70 families. Th ese enzymes are naturally very effi cient transglucosylases. Th ey
use sucrose as substrate and catalyze polymerization of its glucosyl units as a main reaction. Depending on their specifi city,
structures varying in size as well as in glycosidic linkage types can be obtained, thus giving access to an interesting panel of
biopolymers. A campaign of genome sequencing and data mining allowed the isolation of atypical enzymes with new product
specifi cities. In particular, a hyper effi cient polymerase producing a gel-like polymer and, in contrast an enzyme synthesizing
directly from sucrose a polymer of well-controlled low molar mass could be characterized. Structure-function studies combined
with mutagenesis assays allowed us to decipher some of the molecular mechanisms behind the control of the polymer size and
enzyme processivity. Another key property of these catalysts is coming from their ability to glucosylate a broad spectrum of
hydroxylated molecules. Computational protein design, structurally-guided engineering and also random approaches such as
neutral evolution was implemented for a fi ne tuning of their acceptor specifi city toward non-natural acceptors such chemically
protected disaccharides for vaccinal applications, polyol, fl avonoids, or various chemicals. Th ese various approaches will be
described and discussed with regard to the engineering objectives.

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Sergey Suchkov 2 photo

Sergey Suchkov graduated from Astrakhan State Medical University and awarded with MD, then in 1985 maintained his PhD at the I M Sechenov Moscow Medical
Academy and in 2001, he maintained his Doctorship Degree at the Nat Inst of Immunology, Russia. From 1987 through 1989, he was a senior Researcher, Koltzov Inst
of Developmental Biology. From 1989 through 1995, he was a Head of the Lab of Clinical Immunology, Helmholtz Eye research Institute in Moscow. From 1995 through
2004, he was a Chair of the Dept. for Clinical Immunology, Moscow Clinical Research Institute. He has been trained at: NIH; Wills Eye Hospital, PA, USA; Univ. of Florida
in Gainesville; UCSF, S-F, CA, USA; Johns Hopkins University, Baltimore, MD, USA. He was an Exe Secretary-in-Chief of the Editorial Board, Biomedical Science, an
international journal published jointly by the USSR Academy of Sciences and the Royal Society of Chemistry, UK. At present, he is a Chair, Dept. for Personal-ized and
Translational Medicine, I M Sechenov First Moscow State Medical University. He is a member of the New York Academy of Sciences, USA; American Chemical Society
(ACS), USA; American Heart Association (AHA), USA; EPMA (European Association for Predictive, Preventive and Personalized Medicine), Brussels, EU; ARVO (American
Association for Research in Vision and Ophthalmology); ISER (International Society for Eye Re-search); PMC (Personalized Medicine Coalition), Washington, USA.


Personalized medicine (PM) as the healthcare of the future represents an innovative model for advanced healthcare and
robust platform for relevant industrial branches for diagnostics and pharmaceutics. However, rapid market penetration
of new technologies demands the implementation of reforms not only in biopharma, but also in education. Th erefore, the
problem of the updated education of specialists in bioengineering, drug design and affi liated fi elds is becoming particularly
urgent, and it requires signifi cant revision of newer programs and curricula to be updated. Modernization and integration of
widely accepted standards require consolidation of both the natural and medical sciences that may become the conceptual
basis for the biopharma education. Th e main goal of this training is to provide development of novel multifaceted approaches
to build academic schools for future generations. So, a higher, secondary and primary education as a trio should be integrated
into the circuit. Based on current trends and own experience, we have made the fi rst steps towards reshuffl ing the canonical
educational tandem “School-University” and restructuring of specialized groups (with targeted disciplines) to get the mentees
to be involved into having the existing healthcare system advanced and stepped forward. Moreover, non-canonical approach
has been used to create a team of young researchers and biopharma students which has been recognized as Th e International
Research Team of Youngsters under the aegis of EPMA (Brussels, EU) and ISPM (Tokyo, Japan). Th e integration of the primary
and secondary education provides: 1. development in the chosen direction; and 2. optimization of the jointly set activity of a
student and the teacher within a pair or a tandem (mentor-mentee). Th e above-mentioned has pre-determining value, because
under the disintegration of the world community expressed the competition in quality of the scientifi c intellect dramatically
increases. Th e same occurs in the areas of quality of all of three segments of the educational process, i.e., pre-college (secondary
school), university and graduate.

Keynote Forum

David Rabuka

Catalent Biologics, USA

Keynote: Developing site-specifi cally modifi ed ADCs using a chemoenzymatic approach

Time : 11:50-12:30

OMICS International Biotech Congress 2018 International Conference Keynote Speaker David Rabuka photo

We have developed the SMARTagTM technology platform, which enables precise, programmable, site-selective chemical
protein modifi cation. Leveraging the target sequence of formylglycine generating enzyme (FGE), we chemoenzymatically
modify proteins to generate a precisely placed aldehyde functionality that can be chemically elaborated. Subsequently, novel
ligation chemistry is employed that exploits this “aldehyde tag” site. We will present recent data on our novel protein modifi cation
platform and its application to generating novel bioconjugates, including ADCs, utilizing our new conjugation chemistries and
linkers. Th e application of these chemistries to generate site-specifi cally modifi ed bioconjugates with improved effi cacy and
safety profi les will be presented. Additionally, we will highlight the progress in developing conjugates with a focus on preclinical
studies as well as highlight our progress in cell line development and manufacturing by using this chemoenzymatic approach.


David Rabuka received a PhD in Chemistry at the University of California, Berkeley as a Chevron Fellow in the Lab of Carolyn Bertozzi. His research included developing
and applying the SMARTagTM platform technology to cell surface modifi cation. Prior to joining Bertozzi’s lab, he worked at the Burnham Institute synthesizing complex
glycans followed by Optimer Pharmaceuticals, where he focused on the development of glycan and macrolide based antibiotics. He was CSO, President and Co-founder
of Redwood Bioscience, where he developed novel protein conjugation methods and biotherapeutic applications such as antibody-drug conjugates. Redwood Bioscience
was acquired by Catalent Pharma Solutions in Oct 2014, where he has continued to apply the SMARTagTM technology with various collaborators and partners as a Global
Head of R&D. He graduated with a Double Honors BS in Chemistry and Biochemistry from the University of Saskatchewan, where he received the Dean’s Science Award,
and holds an MS in Chemistry From the University of Alberta. He has authored over 45 major publications, as well as numerous book chapters and holds over 30 patents.