The short version of Primary drying fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-01-28. Anything still debated is marked as such rather than presented as settled.
Lyophilization is a dehydration technique in which a product is frozen and the solvent is removed under reduced pressure. The low pressure allows ice to sublimate directly into vapor without passing through a bulk liquid phase. This differs from conventional drying, where heat drives evaporation and can damage heat-sensitive structures. The process is used for biological materials, pharmaceutical formulations, and some foods. Its main advantage is preservation of porous structure and rapid reconstitution.
Freezing is the first stage and sets the ice structure that later becomes the pore network. The formulation is cooled below its freezing point, often with a controlled ramp, and solutes concentrate as ice forms. Primary drying then lowers chamber pressure and supplies heat to sublime the ice. The product temperature must stay below its collapse or eutectic temperature to prevent structural loss. Secondary drying raises the temperature modestly to remove bound water and achieve a low residual moisture.
A freeze-dryer consists of a vacuum chamber, temperature-controlled shelves, a condenser, and a vacuum pump. Vials, ampoules, or bulk trays hold the product during the cycle. The condenser traps water vapor as ice at a temperature lower than the product. Cycle development balances shelf temperature, chamber pressure, and time. Scale-up can be difficult because heat and mass transfer change with equipment size, so process analytical tools and conservative validation are often used.
Storage conditions for dried products usually aim to exclude moisture and oxygen. Vials are sealed under vacuum or with an inert gas, and stoppers must maintain a barrier during transport. Temperature recommendations vary; some materials remain stable at room temperature, while others need refrigeration or frozen storage. Humidity control is critical because dried cakes can absorb water rapidly once a container is opened. Desiccant packs and moisture-barrier bags add further protection during shipping.
Quality control also examines cake structure, color, and reconstitution behavior. A collapsed or shrunken cake can indicate a thermal excursion during drying. Analytical methods such as X-ray diffraction, differential scanning calorimetry, and near-infrared spectroscopy can detect crystallinity or moisture distribution. Regulatory expectations focus on validated assays and lot-to-lot consistency. Questions remain about how well accelerated stability tests predict long-term behavior for every formulation. Visual inspection remains common but is subjective without trained reviewers and reference images.
| Property | Value | Notes |
|---|---|---|
| Common synonyms | freeze-drying, lyophilisation, cryodesiccation | Lyophilization is common in pharmaceutical literature. |
| Typical chamber pressure during primary drying | 0.05–0.5 mbar (5–50 Pa) | Must remain below the triple point of water. |
| Typical shelf temperature during freezing | −40 to −20 °C | Lower temperatures may be used for eutectic systems. |
| Typical residual moisture after secondary drying | 0.5–3% w/w | Product-dependent; low moisture improves stability but can cause over-drying. |
| Typical analytical method for residual moisture | Karl Fischer titration or loss on drying | Thermogravimetric methods are also used. |
The physical chemistry of freezing influences whether a formulation forms an amorphous glass or a crystalline solid. Amorphous systems can collapse if product temperature rises above the glass transition temperature of the freeze concentrate. Crystalline systems may show eutectic melting, where ice and solute melt together at a fixed temperature. Formulators add bulking agents, lyoprotectants, and buffers to preserve structure and biological activity. The optimum cycle keeps product temperature below critical thresholds during primary drying while allowing efficient sublimation.
Lyophilization is a dehydration process that removes water from a frozen material by sublimation under low pressure. The material is first frozen so that water becomes ice; then the surrounding pressure is lowered below the vapor pressure of ice. Heat is applied gently so ice changes directly to vapor without passing through a bulk liquid phase. The vapor is collected on a cold condenser, leaving a dry porous matrix. This process differs from simple evaporation because the material remains frozen during the main drying stage.
The process usually has three stages: freezing, primary drying, and secondary drying. Freezing sets the ice crystal structure and can determine pore size in the final cake. Primary drying removes free ice by sublimation at low pressure and low shelf temperature. Secondary drying removes bound water by raising the shelf temperature, although some water may remain as part of the solid. Cycle parameters depend on formulation, fill volume, vial type, and equipment performance.
Reconstitution involves adding a suitable diluent, often sterile water or a buffer, to the dried cake. Gentle swirling or inversion helps dissolve the material without creating excessive foam. The time required for complete dissolution can range from seconds to several minutes and depends on the cake structure and the diluent. Improper reconstitution, such as vigorous shaking or using the wrong diluent, can cause protein aggregation or loss of activity. After reconstitution, the product may have a limited shelf life and should be used according to its labeling.
Lyophilized products are typically hygroscopic and require protection from moisture during storage. Manufacturers seal them in glass vials, often under vacuum or an inert gas such as nitrogen. The container closure system, including the stopper and crimp seal, must prevent water vapor ingress. Storage temperature varies from controlled room temperature to refrigerated or frozen conditions, depending on the formulation. Humidity-controlled environments are essential because even brief exposure to ambient air can degrade the product.
Freeze-drying is used for materials whose activity or structure depends on low temperature and low water content. Examples include certain biologics, diagnostic reagents, starter cultures, coffee, and porous inorganic precursors. The dried product forms a cake whose porosity aids rapid wetting and dissolution. Main drawbacks are high energy use, long cycle times, and sensitivity to formulation and equipment variation. Questions remain about how freezing rates and ice morphology affect batch uniformity, especially when moving from laboratory to production scale.
Lyophilization, also called freeze-drying, is a dehydration process in which a solvent, usually water, is frozen and then removed by sublimation under reduced pressure. The method preserves heat-sensitive materials that would degrade in conventional drying. Large-scale use grew during the mid-twentieth century for blood plasma and antibiotics, and it later expanded to vaccines, enzymes, foods, and advanced materials. The process produces a dry, porous solid that usually reconstitutes rapidly. It is distinct from simple evaporation because the solvent bypasses the liquid phase during primary removal.
The process generally proceeds in three stages: freezing, primary drying, and secondary drying. During freezing, controlled cooling converts water into ice and may also crystallize or vitrify solutes. In primary drying, the pressure is lowered below the triple point, and heat is supplied so ice sublimes directly to vapor. Secondary drying removes water that remains bound to the solid matrix, yielding a low final water content. Product temperature must stay below the collapse or glass transition temperature to maintain structure. Cycle design therefore balances shelf temperature, chamber pressure, and time.
mRNA display is a method to identify peptides which bind to a particular molecular target. The process utilizes two main components: an immobilized target and a peptide library in which each peptide is covalently linked to an mRNA:cDNA which encodes it. The immobilized target is mixed with the library in a binding step, then those peptide-mRNA:cDNA fusions which do not bind are washed away. The resulting mixture, which is enriched in peptide-mRNA:cDNA fusions that bind, is then amplified via a polymerase chain reaction (PCR). A new peptide library enriched in binding sequences is prepared from this cDNA, and the process is repeated for several rounds. The result is the isolation of nucleotides with sequences that encode peptides with high affinity for the target.
The secretin-cholecystokinin test (aka Secretin-CCK test, Secretin-Pancreozymin test) is a combination of the secretin test and the cholecystokinin test and is used to assess the function of both the pancreas and gall bladder. Cholecystokinin (CKK) is a peptide hormone secreted by I-cells in the intestinal mucosa. It stimulates the secretion of pancreatic fluid into the duodenum through the sphincter of oddi. This fluid is rich in pancreatic enzymes amylase, trypsin, and lipase. It also promotes contraction and relaxation of the gallbladder. Secretin is a peptide hormone that stimulates the secretion of both pancreatic fluid and bicarbonate. The Secretin-cholecystokinin test is considered the gold standard test of pancreatic exocrine function. It is now rarely used in adults in favour of non-invasive tests, though it is still used in some cases in infants with pancreatic insufficiency to distinguish between cystic fibrosis and Schwachman-Diamond syndrome.
From 2002 to 2004, Pinhasov carried out postdoctoral research at Johnson & Johnson Pharmaceutical Research and Development (Spring House, Pennsylvania, United States), where under the guidance of Dr. Douglas Brenneman he was engaged in the development of drugs for the treatment of neurodegenerative diseases. In 2005, Pinhasov joined the Department of Molecular Biology at Ariel University (formerly the College of Judea and Samaria) as an assistant professor. He was Head of the department from 2008 to 2014. In 2014, Pinhasov was appointed Vice-President and Dean of Research & Development at Ariel University, holding this position until 2020. In 2020 the Senate of Ariel University elected Professor Pinhasov as the Rector of Ariel University, succeeding Professor Michael Zinigrad, who held this office for 12 years. In September 2023, in recognition of his contribution to academic ties between Israel and Kazakhstan, the Senate of Astana Medical University (AMU) awarded Prof. Albert Pinhasov the title of honorary professor.
The function of intrinsic termination is to signal for the dissociation of the ternary elongation complex (TEC), which ends transcription and releases RNA polymerase and its associated cofactors as well as the new RNA transcript. Intrinsic termination occurs independently of the protein Rho, in contrast to Rho-dependent termination, where the Rho protein must act on the RNA polymerase in order for it to dissociate from the transcription complex. Here, there is no extra protein and the transcript forms its own loop structure. Intrinsic termination thus regulates the level of transcription as well, determining how many polymerases can transcribe a gene over a given period of time, and can help prevent interactions with neighboring chromosomes.
Sources: en.wikipedia.org
Albert Pinhasov (Hebrew: אלברט פנחסוב; born 9 February 1972) is the Rector of Ariel University. He is a researcher in the fields of Molecular Psychiatry and Psychopharmacology.He also served as Vice President and Dean for Research & Development and the Head of the Department of Molecular Biology at Ariel University. Albert Pinhasov was born on 9 February 1972 in the city of Namangan, Uzbekistan. From 1990 to 1994, he studied at the Gorky Academy of Medicine, in the city of Nizhny Novgorod, Russia. In 1994, he immigrated to Israel where he continued his education at Tel Aviv University. He was awarded a Master of Science degree (MSc) in 1998 and a PhD in the field of Molecular Biology and Clinical Biochemistry under the mentorship of Illana Gozes in 2002 from Tel Aviv University.
Archaeal transcription shares eukaryotic and bacterial ties. With eukaryotes, it shares similarities with its initiation factors that help transcription identify appropriate sequences such as TATA box homologs as well as factors that maintain transcription elongation. However, additional transcription factors similar to those found in bacteria are needed for the whole process to occur. In terms of transcription termination, the archaeal genome is unique in that it is sensitive to both intrinsic termination and factor-dependent termination. Bioinformatic analysis has shown that approximately half of the genes and operons in Archaea arrange themselves into signals or contain signals for intrinsic termination. Archaeal RNA polymerase is responsive to intrinsic signals both in vivo and in vitro such as the poly-U-rich regions. However, unlike bacterial intrinsic termination, no specific RNA structure or hairpin is needed. The surrounding environment and other genome factors can still influence the termination. Factor-dependent termination in archaea is also distinct from factor-dependent termination in bacteria. The terminational factor aCASP1 (also known as FttA) recognizes poly-U-rich regions, probably cooperating with the "intrinsic" mode to achieve more efficient termination.
$40 million for the COVID-19 Genomics Network $23 million for the Vaccine and Infectious Disease Organization-International Vaccine Centre $29 million for the National Research Council of Canada $600 million through the Strategic Innovation Fund $10.3 million over 10 years, $5 million bonus to support the Canadian Immunization Research Network $114.9 million through the Canadian Institutes of Health Research A Vaccine Surveillance Reference Group (VSRG) was also established within the CITF to monitor the safety and effectiveness of COVID-19 vaccines made available in Canada. The task force was to also estimate how many Canadians were immune to the SARS-CoV-2 virus. Catherine Hankins reported that less than 1% of 10,000 samples tested positive for antibodies to SARS-CoV-2. The CITF also found that one in 100 Canadians were infected with COVID-19 during the first wave of the pandemic. Canadian Blood Services analyzed over 30,000 blood samples in total. The CITF Board was composed of doctors, infectious disease experts, and policy makers.
Both the formation and degradation of amylopectin is important to the metabolic processes of organisms. Amylopectin is one of the two dominant components of starch, and starch is a successful storage molecule for energy. Because of this, it is synthesized and broken down in most plants and cyanobacteria. In fact, amylopectin seems to rival glycogen, the energy storage molecule in animals, because it is able to store more glucose units and henceforth more energy. The synthesis of amylopectin depends on the combined efforts of four different enzymes:
In Mexico, the Directorate General of Civil Aviation (DGAC) investigates aviation accidents. In the Netherlands, the Dutch Safety Board (Onderzoeksraad voor Veiligheid) is responsible for the investigation of incidents and accidents, including air accidents. Its aim is the improvement of safety in the Netherlands. Its main focus is on those situations in which civilians are dependent on the government, companies or organizations for their safety. The Board solely investigates when incidents or accidents occur and aims to draw lessons from the results of these investigations. The Safety Board is objective, impartial and independent in its judgment. The Board will always be critical towards all parties concerned.
Sources: en.wikipedia.org
An automated insulin delivery system consists of three distinct components: a continuous glucose monitor to determine blood sugar levels, a pump to deliver insulin, and an algorithm that uses the data from the CGM and pump to determine needed insulin adjustments. In the United States, the Food and Drug Administration (FDA) allows each component to be approved independently, allowing for more rapid approvals and incremental innovation.
The transduction of the signal through the membrane by the receptor is not completely understood. It is known that in the inactive state, the GPCR is bound to a heterotrimeric G protein complex. Binding of an agonist to the GPCR results in a conformational change in the receptor that is transmitted to the bound Gα subunit of the heterotrimeric G protein via protein domain dynamics. The activated Gα subunit exchanges GTP in place of GDP which in turn triggers the dissociation of Gα subunit from the Gβγ dimer and from the receptor. The dissociated Gα and Gβγ subunits interact with other intracellular proteins to continue the signal transduction cascade while the freed GPCR is able to rebind to another heterotrimeric G protein to form a new complex that is ready to initiate another round of signal transduction. It is believed that a receptor molecule exists in a conformational equilibrium between active and inactive biophysical states. The binding of ligands to the receptor may shift the equilibrium toward the active receptor states. Three types of ligands exist: Agonists are ligands that shift the equilibrium in favour of active states; inverse agonists are ligands that shift the equilibrium in favour of inactive states; and neutral antagonists are ligands that do not affect the equilibrium. It is not yet known how exactly the active and inactive states differ from each other.
RGD and other bioactive ligands can be presented on the surface of a biomaterial in a number of different spatial arrangements, and it has been demonstrated that these arrangements have a significant impact on cell behavior. In self-assembled monolayers, it was found that adhesion and proliferation of both human umbilical vein endothelial cells (HUVECs) and human mesenchymal stem cells (MSCs) increased as a function of RGD peptide density. These studies also showed that RGD density could change integrin expression, which has been postulated to enable control of biochemical signaling pathways. Further investigation of MSCs on self-assembled monolayers showed that modulating RGD density and the affinity of RGD for αvβ3 (through use of linear and cyclized RGD) could be used to control the differentiation of MSCs. The effect of RGD presentation on cells in 3D biomaterials, which more accurately replicate the in vivo environment, has also been evaluated. In degradable polyethylene glycol hydrogels, the length of capillary-like structures formed by HUVECs was directly proportional to the density of RGD in the hydrogel. Additionally, studies in nano-patterning have shown that, whereas an increase in global RGD density increases cell adhesion strength until saturation, an increase in local (mico/nano-scale) RGD density does not follow this trend.
From the 17th century, and before modern developments in organic chemistry nomenclature, acetone was given many different names. They included "spirit of Saturn", which was given when it was thought to be a compound of lead and, later, "pyro-acetic spirit" and "pyro-acetic ester". Prior to the name "acetone" being coined by French chemists, it was named "mesit" (from the Greek μεσίτης, meaning mediator) by Carl Reichenbach, who also said that methyl alcohol consisted of mesit and ethyl alcohol. Names derived from mesit include mesitylene and mesityl oxide which were first synthesised from acetone. In 1839, the name "acetone" began to be used, because it was obtained from acetic acid. Unlike many compounds with the acet- prefix which have a 2-carbon chain, acetone has a 3-carbon chain. That has caused confusion because there can not be a ketone with 2 carbons. The prefix refers to acetone's relation to vinegar (acetum in Latin, also the source of the words "acid" and "acetic"), rather than its chemical structure.
Antimicrobial peptides are produced by species across the tree of life, including: bacteria (e.g. bacteriocin, and many others) fungi (e.g. peptaibols, plectasin, and many others) cnidaria (e.g. hydramacin, aurelin) many from insects and arthropods (e.g. cecropin, attacin, melittin, mastoparan, drosomycin, thioester-containing protein 1) amphibia, frogs (magainin, dermaseptin, aurein, and others) birds (e.g. avian defensins) and mammals (e.g. cathelicidins, alpha- and beta-defensins, regIII peptides) Research has increased in recent years to develop artificially-engineered mimics of antimicrobial peptides such as SNAPPs, in part due to the prohibitive cost of producing naturally-derived AMPs. An example of this is the facially cationic peptide C18G, which was designed from the C-terminal domain of human platelet factor IV. Currently, the most widely used antimicrobial peptide is nisin; being the only FDA approved antimicrobial peptide, it is commonly used as an artificial preservative.
Sources: en.wikipedia.org
Yes, the terms are generally interchangeable. Lyophilization is more common in pharmaceutical and laboratory contexts, while freeze-drying appears widely in food science and general writing. Both describe removal of solvent by sublimation under vacuum after freezing.
Reduced pressure keeps the process below the triple point of water, so ice can sublimate directly to vapor. It also lowers the temperature needed for drying, which helps preserve heat-sensitive materials. Without vacuum, melting or boiling could occur instead of controlled sublimation.
The rate depends on heat transfer to the product and mass transfer of vapor through the dried layer. A cold condenser, adequate vacuum, and suitable shelf temperature all influence speed. Formulation properties such as solid content and collapse temperature also set practical limits.
Karl Fischer titration is a common reference method that quantifies water by a chemical reaction. Thermogravimetric analysis can also estimate moisture by weight loss on heating. Method choice depends on sample size and whether other volatile substances are present.