Anionic antimicrobial peptides (AAMPs) have been known to play an important role in the innate immune systems of many different kinds of organisms since their discovery in the 1980s.
Cationic antimicrobial peptides (CAMPs) are peptides recognized for their capacity to target and damage microbial cell membranes.
Cell-penetrating peptides (CPPs) are short oligopeptides of 5 to 30 amino acids, capable of transporting diverse cargos and traversing biological membranes.
Cyclic peptide nanotubes (cPNTs) are tubular entities formed by cyclic peptides that autonomously organize into stable nanotube configurations.
An antibiotic family known as lipoglycopeptides is based on glycopeptides that have lipid side chains added to them to make them more effective against bacteria and have better pharmacokinetics.
The first administration of insulin in 1920 opened the era of therapeutic peptides, and a hundred years later, in 2023, global sales of Semaglutide exceeded 20 billion US dollars, almost forcing K drugs.
A subfield of medical diagnostics known as molecular diagnostics and imaging focuses on visualizing cellular or molecular activities in the body as well as analyzing biological substances.
Drug delivery denotes the administration of pharmacological agents to elicit a therapeutic response within the organism. It includes the formulation, delivery systems, and techniques employed to administer medications into the body, ensuring they arrive at their designated location of action in the correct concentration and duration.
One novel way to cure or prevent disease is through gene therapy, which involves changing a person's genes in their cells. Specifically, it seeks to treat hereditary and mutation-based genetic abnormalities that cause illness. In order to cure a specific condition, gene therapy involves transferring genetic material (DNA or RNA) to repair, control, or replace genes.
Antisense therapy is a molecular strategy that seeks to disrupt gene expression through the use of synthetic oligonucleotides specifically engineered to attach to mRNA transcripts. This binding obstructs the translation of the target protein, hence silencing the gene linked to a certain illness.
Molecular diagnosis and detection is a field within medical and biological sciences that involves the examination of biological markers in the genome (DNA), proteome (proteins), and transcriptome (RNA) to identify diseases, infections, or genetic predispositions.
Over three decades ago, a breakthrough in gene editing—then known as gene targeting—was made when it became possible to build nucleases to produce site-specific DNA double-strand breaks (DSBs), which could increase the rate of homologous recombination (HR) by a factor of over a thousand.
Fluorescence in situ hybridization (FISH) is a technique that does not depend on sequencing. It uses a fluorescently labeled probe, which is either DNA or RNA, with a complementary sequence to the target sequence to hybridize.
A crucial step in molecular biology is nucleic acid purification, which entails extracting RNA or DNA from biological substances. Cloning, sequencing, diagnostics, and gene expression studies are just a few of the many uses that rely on this purification.
Numerous synthetic peptides are notable commercial or medicinal goods, including the dipeptide sugar replacement aspartame and therapeutically used hormones such as oxytocin, adrenocorticotropic hormone, and calcitonin.
Cyclic peptide antibiotics represent a category of antibiotics distinguished by a cyclic configuration, wherein the amino acid sequence creates a loop instead of a linear arrangement.
The construction of cyclic peptides is a potent strategy in drug discovery, biomolecular engineering, and synthetic biology. The process entails the creation of peptides that assume a cyclic conformation, conferring stability, resistance to degradation, and selective binding to molecular targets.
It seems that human beings can no longer be satisfied with cyclic peptides. With the deepening of the exploration and research of cyclic peptides, cyclic peptides have also been gradually subdivided. By classifying from the perspective of amide bonds, homocyclic peptides and heterocyclic peptides can be obtained.
Cyclic peptides are one of the hot concepts in recent years. Compared with linear peptides, some special cyclic peptide structures have the characteristics of high stability and strong targeting, so as to exert stronger efficacy. In addition to synthetic cyclic peptides, plant-derived cyclic peptides are also increasingly appearing in front of the public.
Peptides are a class of molecules that play an important role in living organisms, and are widely used in drug delivery and disease treatment due to their low toxicity, low immunogenicity, high tissue permeability, and easy synthetic modification.
Due to the relative immobilization of the SPPS synthesis process, the generation of peptide impurities has also appeared in a generalized type, and this paper makes a summary introduction to the common types of impurities in the solid-phase synthesis of peptides and the corresponding generation mechanism.
As an important part of drug development, peptide modification has a wide range of modifications and applications. This article will discuss the application of peptide modifications in anticancer, drug delivery, antimicrobial, and multivalent vaccine development, and give relevant examples.
Peptides are composed of amino acids and are highly specific and biocompatible. In modern medical research and clinical applications, peptide modification technology is widely used in the development of diagnostic tools.
With the continuous progress of science and technology, peptide modification technology plays an increasingly important role in the development of scientific research tools. Through various chemical modifications, peptides are not only suitable for technologies such as mass spectrometry and nuclear magnetic resonance, but also help to promote the development of life science research. As a key tool in bioscience research, peptides have shown a wide range of application potential after modification.
With the development of biochemical technology, peptide and peptide modification are more and more widely used in the field of daily chemical products. By changing the physicochemical properties of peptide compounds, peptide modification technology can optimize their effective use in the body and improve their application effect in cosmetics and skin care products.
Peptide modification refers to the modification of peptides by chemical or biotechnological means to improve their performance or give them new functions. In recent years, the application of peptide modification in the field of materials science and biomedicine has received extensive attention.
Peptide modifications play a vital role in basic research. This technology not only helps researchers to deeply explore the structure-function relationship of peptides, but also provides powerful tools and methods in fields such as biomedicine, chemistry, and biotechnology.
Peptide conjugation has been widely used in drug development because of its ability to endow drug molecules with unique structural and functional properties, making it an important strategy for drug development.
In the biomedical field, peptide conjugation is widely used in drug delivery, vaccine development, and tissue engineering. In nanotechnology, the research of peptide functionalized nanoparticles and self-assembling materials is expanding its applications in the fields of diagnostics, therapeutics, and sensors.
Peptide conjugation is an important tool in the field of modern biomedicine, which links peptides with other molecules (such as dyes, drugs, proteins, etc.) through chemical bonds, thus enhancing the application potential of peptides in disease diagnosis. The following are examples of the use of peptide conjugation is used in the diagnosis of several common diseases.
By conjugating peptides to different molecules or materials, researchers have developed advanced scientific tools for biomedical research, drug screening, and molecular imaging. Here are a few examples of the application of peptide conjugation in scientific research tools.
The application of peptide conjugation technology in enzyme engineering provides a new way to improve the stability, activity, and specificity of enzymes. By conjugating peptides to enzyme molecules, enzyme functions can be enhanced and optimized, and their applications in industry, biomedicine, and environmental protection can be expanded.
Cyclic peptides have garnered attention for their unique properties and potential applications in various fields, including cosmetics. These peptides are characterized by their cyclic structure and knotted arrangement of disulfide bonds, which endows them with exceptional stability and bioactivity.
Cyclic peptides, although recently discovered in scientific terms, have roots deeply embedded in the traditional medicine practices of various indigenous communities, particularly in Africa. Historically, cyclic peptide-containing plants like Oldenlandia affinis were revered for their medicinal properties and were integral to the healing rituals and remedies of these communities.
Cyclic peptides are small, disulfide-rich peptides that were originally discovered in plants. Cyclic peptides were initially reported by Seather et al. in 1995, although they had been used in traditional medicine long before that. The first reported cyclic peptide, kalata B1 (kB1), is an active compound in the plant Oldenlandia affinis, used in traditional indigenous medicine in Africa to accelerate childbirth.
RGD peptide is a sequence peptide consisting of three amino acids (Arg-Gly-Asp), which can be divided into linear peptide and cyclic peptide. They are minimally recognized short peptide sequences such as many extracellular matrix proteins such as VN, FN, FGN, collagen, etc.
Cyclic peptides are peptide molecules with a cyclic structure, generally composed of 5-17 amino acids, and with a molecular weight of about 500 Da to 2000 Da. In contrast to linear peptide molecules, cyclic peptide molecules have a stable conformation.
The discovery of insulin a century ago forever changed the field of cyclic peptide drug research. Insulin can be said to be what millions of people with diabetes rely upon today as one of the most influential of drugs, it is a highly complex cyclic peptide hormone, through multiple disulfide bonds together.
At present, a number of cyclic peptide drugs have been used in clinical research, such as romidepsin extracted from Chromobacterium violaceum, which can inhibit histone deacetylase and is used as an anti-tumor drug for the treatment of T cell lymphoma. Cyclosporine, a macro cyclic peptide isolated from cyclosporine, was approved by the FDA in 2021 for the treatment of lupus nephritis (LN).
Currently, the main methods for treating tumors include surgical resection, radiotherapy, and chemotherapy. Chemotherapeutic drugs not only damage tumor cells but also affect a wide range of normal cells, leading to various toxic side effects. The development of resistance to chemotherapy drugs is also a reason why they cannot effectively treat tumors.
Peptides are compounds formed by linking multiple amino acids through peptide bonds, usually consisting of 10-100 amino acid molecules with a relative molecular mass of less than 10,000. Peptides can form a cyclic peptide structure by linking the first and last amino acids together or by forming an intramolecular disulfide bond.
The screening principle of peptide drug screening is to utilize the specific binding between peptide molecules in the peptide library and the target molecules, to screen out peptides with specific biological activities. Various methods of peptide drug screening are described below.
Peptides are low molecular weight protein fragments that play important roles in various life activities. Known active peptides in organisms are mainly produced or obtained from endocrine gland tissues and organs, secretory cells and body fluids, and are closely related to active peptides in cell differentiation, neurohormonal transmitter regulation, tumor lesions, immune regulation, in life activities.
Atrial Natriuretic Peptide (ANP) is a peptide hormone synthesized and released by atrial myocytes. ANP in human blood circulation is composed of 28 amino acid residues, and its receptor is a guanosine cyclase on the cell membrane.
OVA peptides refer to peptides derived from ovalbumin, a component of egg white that consists of several amino acids. Ovalbumin can be prepared by specific enzymatic cleavage into OVA peptides, which have a specific amino acid sequence and are often used as model antigens to study immune cell activation, proliferation and effector functions.
Anti-inflammatory peptides are usually short chain peptides composed of amino acids, which have the ability to reduce inflammatory responses and modulate the immune system. The structure of anti-inflammatory peptides can vary depending on their origin and design.
Peptide phosphorylation is essential to obtain high purity peptides for further characterization, biological research or therapeutic applications.
Peptide purification is essential to obtain high purity peptides for further characterization, biological research or therapeutic applications. It involves isolating the desired peptide from impurities and obtaining high yield and quality purified peptide samples.
Peptide dimers are complexes formed by two peptide chains linked together by chemical bonds. It consists of two identical or different peptide units, which can have the same amino acid sequence or different amino acid sequences.
Peptide chemistry uses different modification strategies to prolong the stability of peptide therapeutics.
The method of using certain hydrolysis methods to break the protein peptide chain of macromolecules to generate small molecular peptides with different activities is protein hydrolysis.
Cell targeting peptides, referred as CTPs, have a good capacity to target the specific targets and thus have potential to deliver payloads specifically.
Peptide-drug conjugate (PDC) is a targeted therapeutic agent that is similar in structure and function to antibody-drug conjugate (ADC). It is made up of connections between different types of peptides and drugs.
Since scientists discovered the first biologically active cyclic peptide (gramicidin S) in 1947, more and more cyclic peptides from marine organisms or microorganisms have attracted researchers' attention for their potential value in the field of medicinal chemistry.
Glycopeptide antibiotics (GPAs) are drugs of last resort for treating severe infections caused by Gram-positive pathogens such as Staphylococcus aureus (SA), Enterococcus spp., and Clostridium difficile.
Peptide bonds, also known as amide bonds, are covalent chemical bonds that link amino acids together in proteins. They are formed through a specific type of reaction called a condensation reaction or dehydration synthesis.
Due to their biocompatibility with proteins, structural diversity, and rigidity, dicyclic peptides are an attractive class of potential therapeutic molecules and are promising as effective alternatives to small molecule and antibody drugs.
Peptides are compounds composed of multiple amino acids linked by peptide bonds in a certain order. They have important biological functions and are the basis of life activities and biomaterial development.
A drug delivery system, the process of getting drugs to their intended target without unleashing toxic side effects on healthy cells, represents an area of great significance in medical research.
Cell penetrating peptides are a class of short peptides with a length of 5~30 amino acids, which can carry polypeptides, nucleic acids, small molecules of drugs and virus particles through cell membranes into cells.
More than 100 neuropeptides have been identified, many of which are known to be hormones but also function as neurotransmitters. Hormones are produced by the endocrine system and neurotransmitters by the nervous system.
Peptides are compounds of α-amino acids linked together by peptide bonds with a molecular weight of less than 10 kDa. It is usually composed of 10-100 amino acid molecules.
Surface plasmon resonance (SPR) technology is an optical sensing technology that can monitor the refractive index change of metal surface with high sensitivity, which is less destructive, free of labeling and real-time monitoring.
Phage display peptide library technology is to fuse gene expression products of exogenous proteins or peptides with phage coat proteins and display them on their surface, and then obtain a large enrichment by screening phages expressing specific peptides or proteins to obtain the target peptide or protein.
Synthetic peptides are a kind of special drugs, which can be regarded as a kind of drugs between small organic molecules and protein macromolecules. Liquid phase synthesis and solid phase synthesis are the main methods of peptide drug synthesis.
In order to improve the antigenic activity of citrullinated peptide chain and overcome the deficiency of linear citrulline peptide chain, Dutch scholar SchellekensGA replaced two serine from the 19 amino acid residues in a citrulline peptide chain with cysteine, and cyclized cysteine to form a disulfide bond similar to the β-rotation structure to form cyclic citrullinated peptide (CCP)
Since the last century, peptides have been widely accepted as drugs. Nearly 100 kinds of peptides have been sold on the market, and a large number of them are under development. In this context, peptide synthesis as a strict field of global pharmaceuticals has been greatly developed.
