2001
DOI: 10.1016/s0921-5107(01)00520-7
|View full text |Cite
|
Sign up to set email alerts
|

Effect of the pH on the piezoelectric properties of collagen films

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

1
4
0
2

Year Published

2003
2003
2024
2024

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 15 publications
(7 citation statements)
references
References 13 publications
1
4
0
2
Order By: Relevance
“…Hickman et al [51], for example, reported the T d (measured by DSC) of fish and bovine collagens as 29.8 and 40.1 • C, respectively. Regarding to collagens films, the literature registered a range from 55.23 to 80.55 • C, for films prepared from bovine serosa [22,46,[52][53][54]. These values reflect the good thermal stability achieved by the Pisces films prepared here.…”
Section: Thermal Analysissupporting
confidence: 59%
See 1 more Smart Citation
“…Hickman et al [51], for example, reported the T d (measured by DSC) of fish and bovine collagens as 29.8 and 40.1 • C, respectively. Regarding to collagens films, the literature registered a range from 55.23 to 80.55 • C, for films prepared from bovine serosa [22,46,[52][53][54]. These values reflect the good thermal stability achieved by the Pisces films prepared here.…”
Section: Thermal Analysissupporting
confidence: 59%
“…Then, is expected higher T d for the collagens with higher content of this imino acid. For collagen films, several other parameters such as solvent, ionic strength, pH, humidity, can contribute to T d values and the analysis becomes more complex [6,42,[46][47][48][49][50].…”
Section: Thermal Analysismentioning
confidence: 99%
“…Moreover thermostability of fish collagen from the internal tissues (swim bladders and bones) was slightly higher than that of pepsin solubilized collagen from the external tissues (fins, scales and skins) [24]. Collagen film prepared from bovine serosa registered a denaturation temperature range from 55.23˚C to 80.55˚C [25] [26]. Moreover the thermal stability of the fish collagen depends on several factors like physiological temperature of the fish, species to which it belongs and has direct correlation with imino acid (proline and hydroxyproline) content.…”
Section: Discussionmentioning
confidence: 96%
“…Within the period D of the microfibrillar assembly, with respect to the native molecule, the increase in negative charge density is established at the extreme ends of the gap and the overlap with the center is highly positive [23]. This hydrolyzed collagen, besides being highly biocompatible [24,25], is quite effective in the treatment of periodontal disease when associated with the guided tissue regeneration technique [26] and the presence of extra carboxylic groups enhances its dielectric properties [27,28].…”
Section: Introductionmentioning
confidence: 99%