Pharmaceutical spray freeze drying

Wanning, Stefan; Süverkrüp, Richard; Lamprecht, Alf

doi:10.1016/j.ijpharm.2015.04.053

Cited by 173 publications

(82 citation statements)

References 115 publications

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“…Interestingly, the solid dispersions prepared by freeze drying offered significantly higher solubility of IND compared to those prepared by of spray drying technique. This might be attributed to the ultra-fast liquid nitrogen freezing followed by a soft and slow freeze drying process preserving the molecular distribution and interactions between IND and BSA molecules (Wanning et al, 2015). Although having the same pH (data not shown), solid dispersions samples displayed higher IND solubility compared to that of the physical mixture samples.…”

Section: Discussionmentioning

confidence: 92%

Efficient approach to enhance drug solubility by particle engineering of bovine serum albumin

Khoder

Abdelkader

ElShaer

et al. 2016

International Journal of Pharmaceutics

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Please cite this article as: Khoder, Mouhamad, Abdelkader, Hamdy, ElShaer, Amr, Karam, Ayman, Najlah, Mohammad, Alany, Raid G., Efficient approach to enhance drug solubility by particle engineering of bovine serum albumin.International Journal of Pharmaceutics http://dx.doi.org/10. 1016/j.ijpharm.2016.11.019 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Section: Discussionmentioning

confidence: 92%

Efficient approach to enhance drug solubility by particle engineering of bovine serum albumin

Khoder

Abdelkader

ElShaer

et al. 2016

International Journal of Pharmaceutics

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“…One of the impediments to using proteins in pharmaceutical formulations has been their inherent instability upon dehydration, as proteins are sensitive to a variety of physical and chemical degradative processes, which are either facilitated or directly mediated by loss of water . Common bioindustrial dehydration processes are lyophilization or freeze‐drying, spray‐drying and microglassification, which may have different effects on the protein integrity. Fourier‐transform infrared (FTIR), Raman and solid state nuclear magnetic resonance (NMR) spectroscopic investigations of several soluble globular proteins have indicated that protein denaturation may be induced by lyophilization, spray‐drying, and precipitation with organic solvents followed by drying .…”

Section: Introductionmentioning

confidence: 99%

Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation

et al. 2017

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Globular proteins composed of different secondary structures and fold types were examined by synchrotron radiation circular dichroism spectroscopy to determine the effects of dehydration on their secondary structures. They exhibited only minor changes upon removal of bulk water during film formation, contrary to previously reported studies of proteins dehydrated by lyophilization (where substantial loss of helical structure and gain in sheet structure was detected). This near lack of conformational change observed for globular proteins contrasts with intrinsically disordered proteins (IDPs) dried in the same manner: the IDPs, which have almost completely unordered structures in solution, exhibited increased amounts of regular (mostly helical) secondary structures when dehydrated, suggesting formation of new intra‐protein hydrogen bonds replacing solvent‐protein hydrogen bonds, in a process which may mimic interactions that occur when IDPs bind to partner molecules. This study has thus shown that the secondary structures of globular and intrinsically disordered proteins behave very differently upon dehydration, and that films are a potentially useful format for examining dehydrated soluble proteins and assessing IDPs structures.

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“…Protein powder, coffee powder, egg albumin, bovine DNAse drugs like, Carbamazepin, Danazole, Trypsinogen, Albuterol sulphate, Ciprofloxacin etc. were manufactured by SFD [62,63,64].…”

Section: Advances In Freeze Drying Techniquementioning

confidence: 99%

An overview of lyophilization: troubleshooting the challenges and pharmaceutical applications

2019

Lett Appl NanoBioSci

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Although, lyophilization is well known technique for drying, recently its applications in pharmaceutical field is tremendously increased. The quality product with low moisture content, higher solubility and easy reconstitution lead to wide spread applications of the process. The formulation is frozen, followed by sublimation and desorption to yield dry powder ready for reconstitution. This technique is critical, therefore optimization of many parameters is mandatory to get quality product. The improper insight of parameters like freezing temperature, drying temperature, vacuum, fill volume, etc. may result into collapse, melt back, blow out, shrinkage of the cake which directly affects product reconstitution time, moisture content, assay, and ultimately the stability of the final product. In this review, the challenges experienced in development of freeze drying cycle and its appropriate remedies are discussed at a length. Additionally pharmaceutical applications with the regulatory concerns are also reviewed.

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Pharmaceutical spray freeze drying

Cited by 173 publications

References 115 publications

Efficient approach to enhance drug solubility by particle engineering of bovine serum albumin

Efficient approach to enhance drug solubility by particle engineering of bovine serum albumin

Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation

An overview of lyophilization: troubleshooting the challenges and pharmaceutical applications

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