2. INTRODUCTION 2 “Proteins which are engineered in the laboratory for pharmaceutical use are referred to as therapeutic proteins” Proteins which are absent or low in individuals with an illness such as Cancer, Infectious diseases, Hemophilia, Anemia, Multiple sclerosis, Hepatitis B/C, etc.
How are therapeutic proteins produced?
Most therapeutic proteins are produced in either Chinese Hamster Ovary (CHO) cell cultures or E. coli fermentations, with a significant number also being produced in Saccharomyces cerevisiae and murine myeloma cells (Rader, 2008)..
What are biotherapeutic proteins?
The term therapeutic protein was first used to describe medicines that are genetically engineered versions of naturally occurring human proteins. The complex structure of proteins can be represented in several different ways to help scientists study larger or smaller details of the molecule..
What are the methods used to produce therapeutic proteins?
Most proteins are produced using recombinant DNA technology using various host systems such as bacteria, yeast, insect cells, and mammalian cells. The host choice is dependent on the cost of production as well as the biological activities that are required for its production..
What is therapeutic protein in biotechnology?
The term therapeutic protein was first used to describe medicines that are genetically engineered versions of naturally occurring human proteins. The complex structure of proteins can be represented in several different ways to help scientists study larger or smaller details of the molecule..
Protein therapeutics can be also grouped based on their molecular types that include antibody-based drugs, anticoagulants, blood factors, bone morphogenetic proteins, engineered protein scaffolds, enzymes, Fc fusion proteins, growth factors, hormones, interferons, interleukins, and thrombolytics (5).
Organized to mimic biotherapeutic product lifecycle. Focuses on the applications of biophysics to different disciplines; in particular, focusing on protein Table of contentsAbout this book
The last few decades have seen the genesis of protein therapeutics, such that these large molecule based drugs comprise an increasingly larger part of the commercial market. Google BooksOriginally published: June 23, 2012
Are protein-based therapies a new paradigm in disease treatment?
Protein-based therapeutics have led to new paradigms in disease treatment. Projected to be half of the top ten selling drugs in 2023, proteins have emerged as rivaling and, in some cases, superior alternatives to historically used small molecule-based medicines.
Are therapeutic protein candidates suitable for drug development?
Therapeutic protein candidates should exhibit favorable properties that render them suitable to become drugs. Nevertheless, there are no well-established guidelines for the efficient selection of proteinaceous molecules with desired features during early stage development. Such guidelines can emerge … .
What are the characteristics of a protein based therapeutic?
These include:
high stability (top left)
ability to enter cells (bottom left)
and appropriate pharmacokinetics (top right) and pharmacodynamics (bottom right). Protein-based therapeutics must also exhibit appropriate pharmacokinetics and pharmacodynamics for optimal function.
Why are protein therapeutics less likely to cause side effects?
Proteins are less likely to cause side effects by interfering with normal biological processes because they have evolved to play highly specific roles. Typically, protein therapeutics show high potency and can also execute more complex functions owing to their intricate three-dimensional structures.
Haem or Heme carrier protein 1 (HCP1) was originally identified as mediating heme-Fe transport although it later emerged that it was the SLC46A1 folate transporter.
Biophysics for therapeutic protein development
Mammalian protein
Parathyroid hormone-related protein (PTHrP) is a proteinaceous hormone and a member of the parathyroid hormone family secreted by mesenchymal stem cells. It is occasionally secreted by cancer cells. However, it also has normal functions in bone, teeth, vascular tissues and other tissues.
Protein phosphorylation is a reversible post-translational modification of proteins
Process of introducing a phosphate group on to a protein
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become either activated or deactivated, or otherwise modifying its function. Approximately 13000 human proteins have sites that are phosphorylated.
Protein splicing is an intramolecular reaction of a
The post-translational removal of peptide sequences from within a protein sequence
Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins on both sides. The splicing junction of the precursor protein is mainly a cysteine or a serine, which are amino acids containing a nucleophilic side chain. The protein splicing reactions which are known now do not require exogenous cofactors or energy sources such as adenosine triphosphate (ATP) or guanosine triphosphate (GTP). Normally, splicing is associated only with pre-mRNA splicing. This precursor protein contains three segments—an N-extein followed by the intein followed by a C-extein. After splicing has taken place, the resulting protein contains the N-extein linked to the C-extein; this splicing product is also termed an extein.
Transforming protein RhoA
Protein and coding gene in humans
Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the RHOA gene. While the effects of RhoA activity are not all well known, it is primarily associated with cytoskeleton regulation, mostly actin stress fibers formation and actomyosin contractility. It acts upon several effectors. Among them, ROCK1 and DIAPH1 are the best described. RhoA, and the other Rho GTPases, are part of a larger family of related proteins known as the Ras superfamily, a family of proteins involved in the regulation and timing of cell division. RhoA is one of the oldest Rho GTPases, with homologues present in the genomes since 1.5 billion years. As a consequence, RhoA is somehow involved in many cellular processes which emerged throughout evolution. RhoA specifically is regarded as a prominent regulatory factor in other functions such as the regulation of cytoskeletal dynamics, transcription, cell cycle progression and cell transformation.
